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Carbonic anhydrase 2 (EC 4.2.1.1) (Carbonate dehydratase II) (Carbonic anhydrase C) (CAC) (Carbonic anhydrase II) (CA-II)

 CAH2_HUMAN              Reviewed;         260 AA.
P00918; B2R7G8; Q6FI12; Q96ET9;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 224.
RecName: Full=Carbonic anhydrase 2;
EC=4.2.1.1;
AltName: Full=Carbonate dehydratase II;
AltName: Full=Carbonic anhydrase C;
Short=CAC;
AltName: Full=Carbonic anhydrase II;
Short=CA-II;
Name=CA2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3108857; DOI=10.1093/nar/15.11.4687;
Montgomery J.C., Venta P.J., Tashian R.E., Hewett-Emmett D.;
"Nucleotide sequence of human liver carbonic anhydrase II cDNA.";
Nucleic Acids Res. 15:4687-4687(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3121496; DOI=10.1016/0888-7543(87)90008-5;
Murakami H., Marelich G.P., Grubb J.H., Kyle J.W., Sly W.S.;
"Cloning, expression, and sequence homologies of cDNA for human
carbonic anhydrase II.";
Genomics 1:159-166(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Urinary bladder;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-260, CLEAVAGE OF INITIATOR METHIONINE, AND
ACETYLATION AT SER-2.
PubMed=4207120;
Lin K.-T.D., Deutsch H.F.;
"Human carbonic anhydrases. XII. The complete primary structure of the
C isozyme.";
J. Biol. Chem. 249:2329-2337(1974).
[8]
PROTEIN SEQUENCE OF 2-260.
PubMed=823150;
Henderson L.E., Henriksson D., Nyman P.O.;
"Primary structure of human carbonic anhydrase C.";
J. Biol. Chem. 251:5457-5463(1976).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
PubMed=3000449; DOI=10.1016/0167-4781(85)90006-5;
Venta P.J., Montgomery J.C., Hewett-Emmett D., Tashian R.E.;
"Comparison of the 5' regions of human and mouse carbonic anhydrase II
genes and identification of possible regulatory elements.";
Biochim. Biophys. Acta 826:195-201(1985).
[10]
INTERACTION WITH SLC4A4.
PubMed=14567693; DOI=10.1021/bi0353124;
Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.;
"Direct extracellular interaction between carbonic anhydrase IV and
the human NBC1 sodium/bicarbonate co-transporter.";
Biochemistry 42:12321-12329(2003).
[11]
INTERACTION WITH SLC4A7.
PubMed=14736710; DOI=10.1152/ajpcell.00382.2003;
Loiselle F.B., Morgan P.E., Alvarez B.V., Casey J.R.;
"Regulation of the human NBC3 Na+/HCO3- cotransporter by carbonic
anhydrase II and PKA.";
Am. J. Physiol. 286:C1423-C1433(2004).
[12]
INTERACTION WITH SLC4A4.
PubMed=15218065; DOI=10.1113/jphysiol.2004.065110;
Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I.,
Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I.;
"Molecular mechanism of kNBC1-carbonic anhydrase II interaction in
proximal tubule cells.";
J. Physiol. (Lond.) 559:55-65(2004).
[13]
FUNCTION, INTERACTION WITH SLC26A6, AND SUBCELLULAR LOCATION.
PubMed=15990874; DOI=10.1038/sj.emboj.7600736;
Alvarez B.V., Vilas G.L., Casey J.R.;
"Metabolon disruption: a mechanism that regulates bicarbonate
transport.";
EMBO J. 24:2499-2511(2005).
[14]
ENZYME REGULATION.
PubMed=17314045; DOI=10.1016/j.bmcl.2007.01.113;
Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S.,
Supuran C.T.;
"Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-
ray crystal structure of the antiviral drug foscarnet complexed to
human carbonic anhydrase I.";
Bioorg. Med. Chem. Lett. 17:2210-2215(2007).
[15]
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=18618712; DOI=10.1002/prot.22144;
Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A.,
Pedone C., Scozzafava A., Supuran C.T., De Simone G.;
"Crystal structure of human carbonic anhydrase XIII and its complex
with the inhibitor acetazolamide.";
Proteins 74:164-175(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-172, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=4621826;
Liljas A., Kannan K.K., Bergsten P.-C., Waara I., Fridborg K.,
Strandberg B., Carlbom U., Jaerup L., Loevgren S., Petef M.;
"Crystal structure of human carbonic anhydrase C.";
Nature New Biol. 235:131-137(1972).
[19]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC ION.
PubMed=3151019; DOI=10.1002/prot.340040406;
Eriksson A.E., Jones T.A., Liljas A.;
"Refined structure of human carbonic anhydrase II at 2.0-A
resolution.";
Proteins 4:274-282(1988).
[20]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
INHIBITORS.
PubMed=3151020; DOI=10.1002/prot.340040407;
Eriksson A.E., Kylsten P.M., Jones T.A., Liljas A.;
"Crystallographic studies of inhibitor binding sites in human carbonic
anhydrase II: a pentacoordinated binding of the SCN-ion to the zinc at
high pH.";
Proteins 4:283-293(1988).
[21]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT SER-199 IN COMPLEX
WITH ZINC ION, MUTAGENESIS OF THR-199, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=1909891; DOI=10.1021/bi00102a005;
Krebs J.F., Fierke C.A., Alexander R.S., Christianson D.W.;
"Conformational mobility of His-64 in the Thr-200TO: human carbonic
anhydrase II.";
Biochemistry 30:9153-9160(1991).
[22]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANTS PHE-142; TYR-142 AND
HIS-142 IN COMPLEX WITH INHIBITORS, AND MUTAGENESIS OF VAL-142.
PubMed=1932029; DOI=10.1021/bi00110a008;
Alexander R.S., Nair S.K., Christianson D.W.;
"Engineering the hydrophobic pocket of carbonic anhydrase II.";
Biochemistry 30:11064-11072(1991).
[23]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF MUTANT ALA-121, MUTAGENESIS
OF VAL-121, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=1910042;
Nair S.K., Calderone T.L., Christianson D.W., Fierke C.A.;
"Altering the mouth of a hydrophobic pocket. Structure and kinetics of
human carbonic anhydrase II mutants at residue Val-121.";
J. Biol. Chem. 266:17320-17325(1991).
[24]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
INHIBITORS, AND ENZYME REGULATION.
PubMed=1336460; DOI=10.1111/j.1432-1033.1992.tb17490.x;
Mangani S., Haakansson K.;
"Crystallographic studies of the binding of protonated and
unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide
and nitrate anions.";
Eur. J. Biochem. 210:867-871(1992).
[25]
X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
INHIBITORS.
PubMed=1433293; DOI=10.1016/0022-2836(92)90531-N;
Haakansson K., Carlsson M., Svensson L.A., Liljas A.;
"Structure of native and apo carbonic anhydrase II and structure of
some of its anion-ligand complexes.";
J. Mol. Biol. 227:1192-1204(1992).
[26]
X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH COBALT ION AND
BICARBONATE.
PubMed=1474587; DOI=10.1016/0022-2836(92)90327-G;
Haakansson K., Wehnert A.;
"Structure of cobalt carbonic anhydrase complexed with bicarbonate.";
J. Mol. Biol. 228:1212-1218(1992).
[27]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT CYS-94 IN COMPLEX
WITH ZINC ION, AND MUTAGENESIS OF HIS-94.
PubMed=8431430; DOI=10.1021/bi00057a015;
Alexander R.S., Kiefer L.L., Fierke C.A., Christianson D.W.;
"Engineering the zinc binding site of human carbonic anhydrase II:
structure of the His-94-->Cys apoenzyme in a new crystalline form.";
Biochemistry 32:1510-1518(1993).
[28]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT ALA-197; GLU-197;
HIS-197 AND ARG-197, AND MUTAGENESIS OF LEU-197.
PubMed=8485129; DOI=10.1021/bi00068a005;
Nair S.K., Christianson D.W.;
"Structural consequences of hydrophilic amino acid substitutions in
the hydrophobic pocket of human carbonic anhydrase II.";
Biochemistry 32:4506-4514(1993).
[29]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT CYS-198 IN COMPLEX
WITH ZINC ION, AND MUTAGENESIS OF THR-198.
PubMed=8399159; DOI=10.1021/bi00089a005;
Ippolito J.A., Christianson D.W.;
"Structure of an engineered His3Cys zinc binding site in human
carbonic anhydrase II.";
Biochemistry 32:9901-9905(1993).
[30]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT ALA-201 IN COMPLEX
WITH ZINC ION, AND MUTAGENESIS OF PRO-201.
PubMed=8218160; DOI=10.1021/bi00092a003;
Tweedy N.B., Nair S.K., Paterno S.A., Fierke C.A., Christianson D.W.;
"Structure and energetics of a non-proline cis-peptidyl linkage in a
proline-202-->alanine carbonic anhydrase II variant.";
Biochemistry 32:10944-10949(1993).
[31]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
INHIBITORS.
PubMed=8482389; DOI=10.1016/0014-5793(93)81565-H;
Joensson B.M., Haakansson K., Liljas A.;
"The structure of human carbonic anhydrase II in complex with bromide
and azide.";
FEBS Lett. 322:186-190(1993).
[32]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT VAL-198 IN COMPLEX
WITH ZINC ION AND INHIBITORS, MUTAGENESIS OF THR-198, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8262987;
Krebs J.F., Ippolito J.A., Christianson D.W., Fierke C.A.;
"Structural and functional importance of a conserved hydrogen bond
network in human carbonic anhydrase II.";
J. Biol. Chem. 268:27458-27466(1993).
[33]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND
ZINC ION.
PubMed=8331673; DOI=10.1006/jmbi.1993.1365;
Mangani S., Liljas A.;
"Crystal structure of the complex between human carbonic anhydrase II
and the aromatic inhibitor 1,2,4-triazole.";
J. Mol. Biol. 232:9-14(1993).
[34]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT HIS-199 IN COMPLEX
WITH BICARBONATE AND ZINC ION, AND MUTAGENESIS OF THR-199.
PubMed=8451242; DOI=10.1002/prot.340150110;
Xue Y., Vidgren J., Svensson L.A., Liljas A., Jonsson B.H.,
Lindskog S.;
"Crystallographic analysis of Thr-200-->His human carbonic anhydrase
II and its complex with the substrate, HCO3-.";
Proteins 15:80-87(1993).
[35]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANTS IN COMPLEX WITH
BICARBONATE AND ZINC ION, AND MUTAGENESIS OF GLU-106 AND THR-198.
PubMed=7901850; DOI=10.1002/prot.340170112;
Xue Y., Liljas A., Jonsson B.H., Lindskog S.;
"Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen-
bond network in human carbonic anhydrase II.";
Proteins 17:93-106(1993).
[36]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH COBALT; COPPER;
NICKEL AND MANGANESE IONS.
PubMed=15299481; DOI=10.1107/S0907444993008790;
Haakansson K., Wehnert A., Liljas A.;
"X-ray analysis of metal-substituted human carbonic anhydrase II
derivatives.";
Acta Crystallogr. D 50:93-100(1994).
[37]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) MUTANT GLN-106 IN COMPLEX WITH
THE INHIBITOR ACETATE, AND MUTAGENESIS OF GLU-106.
PubMed=15299482; DOI=10.1107/S0907444993009667;
Haakansson K., Briand C., Zaitsev V., Xue Y., Liljas A.;
"Wild-type and E106Q mutant carbonic anhydrase complexed with
acetate.";
Acta Crystallogr. D 50:101-104(1994).
[38]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-259 OF MUTANTS ALA-94;
CYS-94; CYS-96; CYS-119 AND ASP-119 IN COMPLEX WITH ZINC ION.
PubMed=7803386; DOI=10.1021/bi00255a004;
Ippolito J.A., Christianson D.W.;
"Structural consequences of redesigning a protein-zinc binding site.";
Biochemistry 33:15241-15249(1994).
[39]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
TRIFLUOROMETHANE SULPHONAMIDE.
PubMed=8070585; DOI=10.1016/0014-5793(94)00798-5;
Haakansson K., Liljas A.;
"The structure of a complex between carbonic anhydrase II and a new
inhibitor, trifluoromethane sulphonamide.";
FEBS Lett. 350:319-322(1994).
[40]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=8142888; DOI=10.1002/pro.5560030115;
Smith G.M., Alexander R.S., Christianson D.W., McKeever B.M.,
Ponticello G.S., Springer J.P., Randall W.C., Baldwin J.J.,
Habecker C.N.;
"Positions of His-64 and a bound water in human carbonic anhydrase II
upon binding three structurally related inhibitors.";
Protein Sci. 3:118-125(1994).
[41]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS ARG-197; ASP-197 AND
PHE-197 IN COMPLEX WITH THE INHIBITOR ACETAZOLAMIDE.
PubMed=7696263; DOI=10.1021/bi00012a016;
Nair S.K., Krebs J.F., Christianson D.W., Fierke C.A.;
"Structural basis of inhibitor affinity to variants of human carbonic
anhydrase II.";
Biochemistry 34:3981-3989(1995).
[42]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=7608893; DOI=10.1021/jm00013a004;
Boriack P.A., Christianson D.W., Kingery-Wood J., Whitesides G.M.;
"Secondary interactions significantly removed from the sulfonamide
binding pocket of carbonic anhydrase II influence inhibitor binding
constants.";
J. Med. Chem. 38:2286-2291(1995).
[43]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANTS ASP-198; GLU-198 AND
HIS-198 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF THR-198, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7761440; DOI=10.1073/pnas.92.11.5017;
Ippolito J.A., Baird T.T. Jr., McGee S.A., Christianson D.W.,
Fierke C.A.;
"Structure-assisted redesign of a protein-zinc-binding site with
femtomolar affinity.";
Proc. Natl. Acad. Sci. U.S.A. 92:5017-5021(1995).
[44]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF THE MUTANT GLN-117 IN
COMPLEX WITH ZINC ION AND THE INHIBITOR ACETAZOLAMIDE, AND MUTAGENESIS
OF GLU-117.
PubMed=8639494; DOI=10.1021/bi9526692;
Huang C.C., Lesburg C.A., Kiefer L.L., Fierke C.A., Christianson D.W.;
"Reversal of the hydrogen bond to zinc ligand histidine-119
dramatically diminishes catalysis and enhances metal equilibration
kinetics in carbonic anhydrase II.";
Biochemistry 35:3439-3446(1996).
[45]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS GLY-65; HIS-65;
LEU-65; PHE-65; SER-65 AND THR-65 IN COMPLEX WITH ZINC ION.
PubMed=8987974; DOI=10.1021/bi9617872;
Scolnick L.R., Christianson D.W.;
"X-ray crystallographic studies of alanine-65 variants of carbonic
anhydrase II reveal the structural basis of compromised proton
transfer in catalysis.";
Biochemistry 35:16429-16434(1996).
[46]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
DANSYLAMIDE.
PubMed=8557623; DOI=10.1074/jbc.271.2.1003;
Nair S.K., Elbaum D., Christianson D.W.;
"Unexpected binding mode of the sulfonamide fluorophore 5-
dimethylamino-1-naphthalene sulfonamide to human carbonic anhydrase
II. Implications for the development of a zinc biosensor.";
J. Biol. Chem. 271:1003-1007(1996).
[47]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH THE ACTIVATOR
HISTAMINE, AND ENZYME REGULATION.
PubMed=9265618; DOI=10.1021/bi970760v;
Briganti F., Mangani S., Orioli P., Scozzafava A., Vernaglione G.,
Supuran C.T.;
"Carbonic anhydrase activators: X-ray crystallographic and
spectroscopic investigations for the interaction of isozymes I and II
with histamine.";
Biochemistry 36:10384-10392(1997).
[48]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANTS ASN-94; ASN-119 AND
GLN-119 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF HIS-94 AND HIS-119,
AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=9398308; DOI=10.1021/bi971296x;
Lesburg C.A., Huang C., Christianson D.W., Fierke C.A.;
"Histidine --> carboxamide ligand substitutions in the zinc binding
site of carbonic anhydrase II alter metal coordination geometry but
retain catalytic activity.";
Biochemistry 36:15780-15791(1997).
[49]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
BRINZOLAMIDE.
PubMed=9541386; DOI=10.1002/pro.5560070303;
Stams T., Chen Y., Boriack-Sjodin P.A., Hurt J.D., Liao J., May J.A.,
Dean T., Laipis P., Silverman D.N., Christianson D.W.;
"Structures of murine carbonic anhydrase IV and human carbonic
anhydrase II complexed with brinzolamide: molecular basis of isozyme-
drug discrimination.";
Protein Sci. 7:556-563(1998).
[50]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH SULFONAMIDE
INHIBITORS AND ZINC ION.
PubMed=9865942; DOI=10.1002/pro.5560071201;
Boriack-Sjodin P.A., Zeitlin S., Chen H.H., Crenshaw L., Gross S.,
Dantanarayana A., Delgado P., May J.A., Dean T., Christianson D.W.;
"Structural analysis of inhibitor binding to human carbonic anhydrase
II.";
Protein Sci. 7:2483-2489(1998).
[51]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CYANAMIDE AND
SUBSTRATE, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10550681; DOI=10.1007/s007750050375;
Briganti F., Mangani S., Scozzafava A., Vernaglione G., Supuran C.T.;
"Carbonic anhydrase catalyzes cyanamide hydration to urea: is it
mimicking the physiological reaction?";
J. Biol. Inorg. Chem. 4:528-536(1999).
[52]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH CYANAMIDE.
PubMed=11015219; DOI=10.1021/bi000937c;
Guerri A., Briganti F., Scozzafava A., Supuran C.T., Mangani S.;
"Mechanism of cyanamide hydration catalyzed by carbonic anhydrase II
suggested by cryogenic X-ray diffraction.";
Biochemistry 39:12391-12397(2000).
[53]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTANTS ILE-93/MET-95/VAL-97
AND SER-93/LEU-95/MET-97 IN COMPLEX WITH COBALT; COPPER AND ZINC IONS.
PubMed=11076507; DOI=10.1021/bi001649j;
Cox J.D., Hunt J.A., Compher K.M., Fierke C.A., Christianson D.W.;
"Structural influence of hydrophobic core residues on metal binding
and specificity in carbonic anhydrase II.";
Biochemistry 39:13687-13694(2000).
[54]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX
WITH 4-METHYLIMIDAZOLE, AND MUTAGENESIS OF HIS-64.
PubMed=11327835; DOI=10.1021/bi002295z;
Duda D., Tu C., Qian M., Laipis P., Agbandje-McKenna M.,
Silverman D.N., McKenna R.;
"Structural and kinetic analysis of the chemical rescue of the proton
transfer function of carbonic anhydrase II.";
Biochemistry 40:1741-1748(2001).
[55]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT VAL-130 IN COMPLEX
WITH FLUOROAROMATIC INHIBITORS.
PubMed=11572683; DOI=10.1021/ja011034p;
Kim C.Y., Chandra P.P., Jain A., Christianson D.W.;
"Fluoroaromatic-fluoroaromatic interactions between inhibitors bound
in the crystal lattice of human carbonic anhydrase II.";
J. Am. Chem. Soc. 123:9620-9627(2001).
[56]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
SUGAR SULFAMATE RWJ-37497, AND ENZYME REGULATION.
PubMed=11802772; DOI=10.1042/0264-6021:3610437;
Recacha R., Costanzo M.J., Maryanoff B.E., Chattopadhyay D.;
"Crystal structure of human carbonic anhydrase II complexed with an
anti-convulsant sugar sulphamate.";
Biochem. J. 361:437-441(2002).
[57]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF THE MUTANT PRO-198/SER-205
IN COMPLEX WITH BICARBONATE AND INHIBITORS, AND MUTAGENESIS OF
THR-198.
PubMed=12056894; DOI=10.1021/bi020053o;
Huang S., Sjoeblom B., Sauer-Eriksson A.E., Jonsson B.H.;
"Organization of an efficient carbonic anhydrase: implications for the
mechanism based on structure-function studies of a T199P/C206S
mutant.";
Biochemistry 41:7628-7635(2002).
[58]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF THE MUTANT HIS-7, AND
MUTAGENESIS OF TYR-7.
PubMed=12171926; DOI=10.1074/jbc.M205791200;
Tu C., Qian M., An H., Wadhwa N.R., Duda D., Yoshioka C., Pathak Y.,
McKenna R., Laipis P.J., Silverman D.N.;
"Kinetic analysis of multiple proton shuttles in the active site of
human carbonic anhydrase.";
J. Biol. Chem. 277:38870-38876(2002).
[59]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
FUNCTION.
PubMed=11831900; DOI=10.1021/jm010163d;
Kim C.Y., Whittington D.A., Chang J.S., Liao J., May J.A.,
Christianson D.W.;
"Structural aspects of isozyme selectivity in the binding of
inhibitors to carbonic anhydrases II and IV.";
J. Med. Chem. 45:888-893(2002).
[60]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=12166932; DOI=10.1021/jm011112j;
Grueneberg S., Stubbs M.T., Klebe G.;
"Successful virtual screening for novel inhibitors of human carbonic
anhydrase: strategy and experimental confirmation.";
J. Med. Chem. 45:3588-3602(2002).
[61]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=11818565; DOI=10.1073/pnas.032673399;
Grzybowski B.A., Ishchenko A.V., Kim C.Y., Topalov G., Chapman R.,
Christianson D.W., Whitesides G.M., Shakhnovich E.I.;
"Combinatorial computational method gives new picomolar ligands for a
known enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 99:1270-1273(2002).
[62]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX
WITH THE INHIBITOR 4-METHYLIMIDAZOLE AND ZINC ION.
PubMed=12499545;
Duda D., Govindasamy L., Agbandje-McKenna M., Tu C., Silverman D.N.,
McKenna R.;
"The refined atomic structure of carbonic anhydrase II at 1.05 A
resolution: implications of chemical rescue of proton transfer.";
Acta Crystallogr. D 59:93-104(2003).
[63]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
ENZYME REGULATION.
PubMed=14736236; DOI=10.1021/jm030912m;
Weber A., Casini A., Heine A., Kuhn D., Supuran C.T., Scozzafava A.,
Klebe G.;
"Unexpected nanomolar inhibition of carbonic anhydrase by COX-2-
selective celecoxib: new pharmacological opportunities due to related
binding site recognition.";
J. Med. Chem. 47:550-557(2004).
[64]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THE ANTI-CANCER
AGENT 667-COUMATE.
PubMed=15453828; DOI=10.1042/BJ20041037;
Lloyd M.D., Pederick R.L., Natesh R., Woo L.W., Purohit A., Reed M.J.,
Acharya K.R., Potter B.V.;
"Crystal structure of human carbonic anhydrase II at 1.95 A resolution
in complex with 667-coumate, a novel anti-cancer agent.";
Biochem. J. 385:715-720(2005).
[65]
X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), MUTAGENESIS OF ASN-62; HIS-64
AND ASN-67, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15667203; DOI=10.1021/bi0480279;
Fisher Z., Hernandez Prada J.A., Tu C., Duda D., Yoshioka C., An H.,
Govindasamy L., Silverman D.N., McKenna R.;
"Structural and kinetic characterization of active-site histidine as a
proton shuttle in catalysis by human carbonic anhydrase II.";
Biochemistry 44:1097-1105(2005).
[66]
X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH DUAL
AROMATASE-STEROID SULFATASE INHIBITORS.
PubMed=15865431; DOI=10.1021/bi047692e;
Lloyd M.D., Thiyagarajan N., Ho Y.T., Woo L.W., Sutcliffe O.B.,
Purohit A., Reed M.J., Acharya K.R., Potter B.V.;
"First crystal structures of human carbonic anhydrase II in complex
with dual aromatase-steroid sulfatase inhibitors.";
Biochemistry 44:6858-6866(2005).
[67]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACTIVATOR
L-HISTIDINE, AND ENZYME REGULATION.
PubMed=16214338; DOI=10.1016/j.bmcl.2005.08.069;
Temperini C., Scozzafava A., Puccetti L., Supuran C.T.;
"Carbonic anhydrase activators: X-ray crystal structure of the adduct
of human isozyme II with L-histidine as a platform for the design of
stronger activators.";
Bioorg. Med. Chem. Lett. 15:5136-5141(2005).
[68]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=16134940; DOI=10.1021/jm050333c;
Menchise V., De Simone G., Alterio V., Di Fiore A., Pedone C.,
Scozzafava A., Supuran C.T.;
"Carbonic anhydrase inhibitors: stacking with Phe131 determines active
site binding region of inhibitors as exemplified by the X-ray crystal
structure of a membrane-impermeant antitumor sulfonamide complexed
with isozyme II.";
J. Med. Chem. 48:5721-5727(2005).
[69]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), AND MUTAGENESIS OF HIS-64 AND
THR-199.
PubMed=16106378; DOI=10.1002/prot.20615;
Bhatt D., Tu C., Fisher S.Z., Hernandez Prada J.A., McKenna R.,
Silverman D.N.;
"Proton transfer in a Thr200His mutant of human carbonic anhydrase
II.";
Proteins 61:239-245(2005).
[70]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
PubMed=16511248; DOI=10.1107/S1744309105038248;
Budayova-Spano M., Fisher S.Z., Dauvergne M.T., Agbandje-McKenna M.,
Silverman D.N., Myles D.A., McKenna R.;
"Production and X-ray crystallographic analysis of fully deuterated
human carbonic anhydrase II.";
Acta Crystallogr. F 62:6-9(2006).
[71]
X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=16820676; DOI=10.1107/S1744309106020446;
Fisher S.Z., Govindasamy L., Boyle N., Agbandje-McKenna M.,
Silverman D.N., Blackburn G.M., McKenna R.;
"X-ray crystallographic studies reveal that the incorporation of
spacer groups in carbonic anhydrase inhibitors causes alternate
binding modes.";
Acta Crystallogr. F 62:618-622(2006).
[72]
X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS
VALDECOXIB AND CELECOXIB, AND ENZYME REGULATION.
PubMed=16290146; DOI=10.1016/j.bmcl.2005.09.040;
Di Fiore A., Pedone C., D'Ambrosio K., Scozzafava A., De Simone G.,
Supuran C.T.;
"Carbonic anhydrase inhibitors: Valdecoxib binds to a different active
site region of the human isoform II as compared to the structurally
related cyclooxygenase II 'selective' inhibitor celecoxib.";
Bioorg. Med. Chem. Lett. 16:437-442(2006).
[73]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH N-HYDROXYUREA,
AND ENZYME REGULATION.
PubMed=16759856; DOI=10.1016/j.bmcl.2006.05.068;
Temperini C., Innocenti A., Scozzafava A., Supuran C.T.;
"N-hydroxyurea -- a versatile zinc binding function in the design of
metalloenzyme inhibitors.";
Bioorg. Med. Chem. Lett. 16:4316-4320(2006).
[74]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=17000110; DOI=10.1016/j.bmcl.2006.09.022;
Menchise V., De Simone G., Di Fiore A., Scozzafava A., Supuran C.T.;
"Carbonic anhydrase inhibitors: X-ray crystallographic studies for the
binding of 5-amino-1,3,4-thiadiazole-2-sulfonamide and 5-(4-amino-3-
chloro-5-fluorophenylsulfonamido)-1,3,4-thiadiazole-2-sulfonamide to
human isoform II.";
Bioorg. Med. Chem. Lett. 16:6204-6208(2006).
[75]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH L- AND
D-HISTIDINE, AND ENZYME REGULATION.
PubMed=16807956; DOI=10.1002/chem.200600159;
Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
"Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA,
VII, and XIV with l- and d-histidine and crystallographic analysis of
their adducts with isoform II: engineering proton-transfer processes
within the active site of an enzyme.";
Chemistry 12:7057-7066(2006).
[76]
X-RAY CRYSTALLOGRAPHY (0.99 ANGSTROMS) IN COMPLEX WITH TWO-PRONG
INHIBITORS.
PubMed=16506782; DOI=10.1021/ja057257n;
Jude K.M., Banerjee A.L., Haldar M.K., Manokaran S., Roy B.,
Mallik S., Srivastava D.K., Christianson D.W.;
"Ultrahigh resolution crystal structures of human carbonic anhydrases
I and II complexed with 'two-prong' inhibitors reveal the molecular
basis of high affinity.";
J. Am. Chem. Soc. 128:3011-3018(2006).
[77]
X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=16787097; DOI=10.1021/ja061574s;
Alterio V., Vitale R.M., Monti S.M., Pedone C., Scozzafava A.,
Cecchi A., De Simone G., Supuran C.T.;
"Carbonic anhydrase inhibitors: X-ray and molecular modeling study for
the interaction of a fluorescent antitumor sulfonamide with isozyme II
and IX.";
J. Am. Chem. Soc. 128:8329-8335(2006).
[78]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH L- AND
D-PHENYLALANINE, AND ENZYME REGULATION.
PubMed=16686544; DOI=10.1021/jm0603320;
Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
"Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA,
VII, and XIV with L- and D-phenylalanine and crystallographic analysis
of their adducts with isozyme II: stereospecific recognition within
the active site of an enzyme and its consequences for the drug
design.";
J. Med. Chem. 49:3019-3027(2006).
[79]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=16942027; DOI=10.1021/jm060531j;
De Simone G., Vitale R.M., Di Fiore A., Pedone C., Scozzafava A.,
Montero J.-L., Winum J.-Y., Supuran C.T.;
"Carbonic anhydrase inhibitors: Hypoxia-activatable sulfonamides
incorporating disulfide bonds that target the tumor-associated isoform
IX.";
J. Med. Chem. 49:5544-5551(2006).
[80]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=17125255; DOI=10.1021/jm060807n;
Winum J.Y., Temperini C., El Cheikh K., Innocenti A., Vullo D.,
Ciattini S., Montero J.-L., Scozzafava A., Supuran C.T.;
"Carbonic anhydrase inhibitors: clash with Ala65 as a means for
designing inhibitors with low affinity for the ubiquitous isozyme II,
exemplified by the crystal structure of the topiramate sulfamide
analogue.";
J. Med. Chem. 49:7024-7031(2006).
[81]
X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=17181151; DOI=10.1021/jm060705x;
Leese M.P., Leblond B., Smith A., Newman S.P., Di Fiore A.,
De Simone G., Supuran C.T., Purohit A., Reed M.J., Potter B.V.;
"2-substituted estradiol bis-sulfamates, multitargeted antitumor
agents: synthesis, in vitro SAR, protein crystallography, and in vivo
activity.";
J. Med. Chem. 49:7683-7696(2006).
[82]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SACCHARIN, AND
ENZYME REGULATION.
PubMed=17705204; DOI=10.1002/anie.200701189;
Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A.,
Heine A., Supuran C.T., Klebe G.;
"Saccharin inhibits carbonic anhydrases: possible explanation for its
unpleasant metallic aftertaste.";
Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007).
[83]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
PubMed=17319692; DOI=10.1021/bi062066y;
Fisher S.Z., Maupin C.M., Budayova-Spano M., Govindasamy L., Tu C.,
Agbandje-McKenna M., Silverman D.N., Voth G.A., McKenna R.;
"Atomic crystal and molecular dynamics simulation structures of human
carbonic anhydrase II: insights into the proton transfer mechanism.";
Biochemistry 46:2930-2937(2007).
[84]
X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), MUTAGENESIS OF TYR-7; ASN-62
AND ASN-67, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17330962; DOI=10.1021/bi602620k;
Fisher S.Z., Tu C., Bhatt D., Govindasamy L., Agbandje-McKenna M.,
McKenna R., Silverman D.N.;
"Speeding up proton transfer in a fast enzyme: kinetic and
crystallographic studies on the effect of hydrophobic amino acid
substitutions in the active site of human carbonic anhydrase II.";
Biochemistry 46:3803-3813(2007).
[85]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ACTIVATOR
L-ADRENALINE, AND ENZYME REGULATION.
PubMed=17127057; DOI=10.1016/j.bmcl.2006.11.027;
Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A.,
Supuran C.T.;
"Carbonic anhydrase activators: L-Adrenaline plugs the active site
entrance of isozyme II, activating better isoforms I, IV, VA, VII, and
XIV.";
Bioorg. Med. Chem. Lett. 17:628-635(2007).
[86]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=17251017; DOI=10.1016/j.bmcl.2006.12.099;
Di Fiore A., Scozzafava A., Winum J.-Y., Montero J.-L., Pedone C.,
Supuran C.T., De Simone G.;
"Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-
sulfanilamide derivative to human isoform II and its consequences for
the drug design of enzyme inhibitors incorporating sugar moieties.";
Bioorg. Med. Chem. Lett. 17:1726-1731(2007).
[87]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR
N-HYDROXYSULFAMIDE.
PubMed=17346964; DOI=10.1016/j.bmcl.2007.02.068;
Temperini C., Winum J.Y., Montero J.L., Scozzafava A., Supuran C.T.;
"Carbonic anhydrase inhibitors: the X-ray crystal structure of the
adduct of N-hydroxysulfamide with isozyme II explains why this new
zinc binding function is effective in the design of potent
inhibitors.";
Bioorg. Med. Chem. Lett. 17:2795-2801(2007).
[88]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
ENZYME REGULATION.
PubMed=17540563; DOI=10.1016/j.bmcl.2007.05.045;
Alterio V., De Simone G., Monti S.M., Scozzafava A., Supuran C.T.;
"Carbonic anhydrase inhibitors: inhibition of human, bacterial, and
archaeal isozymes with benzene-1,3-disulfonamides -- solution and
crystallographic studies.";
Bioorg. Med. Chem. Lett. 17:4201-4207(2007).
[89]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
ENZYME REGULATION.
PubMed=17588751; DOI=10.1016/j.bmcl.2007.06.044;
Temperini C., Innocenti A., Mastrolorenzo A., Scozzafava A.,
Supuran C.T.;
"Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug
sulthiame with twelve mammalian isoforms: kinetic and X-ray
crystallographic studies.";
Bioorg. Med. Chem. Lett. 17:4866-4872(2007).
[90]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH
4-METHYLIMIDAZOLE, AND MUTAGENESIS OF TRP-5 AND HIS-64.
PubMed=17071654; DOI=10.1529/biophysj.106.093203;
Bhatt D., Fisher S.Z., Tu C., McKenna R., Silverman D.N.;
"Location of binding sites in small molecule rescue of human carbonic
anhydrase II.";
Biophys. J. 92:562-570(2007).
[91]
X-RAY CRYSTALLOGRAPHY (1.01 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=17407288; DOI=10.1021/ja068359w;
Srivastava D.K., Jude K.M., Banerjee A.L., Haldar M., Manokaran S.,
Kooren J., Mallik S., Christianson D.W.;
"Structural analysis of charge discrimination in the binding of
inhibitors to human carbonic anhydrases I and II.";
J. Am. Chem. Soc. 129:5528-5537(2007).
[92]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITOR
THIOXOLONE, AND ENZYME REGULATION.
PubMed=18266323; DOI=10.1021/bi702385k;
Barrese A.A. III, Genis C., Fisher S.Z., Orwenyo J.N., Kumara M.T.,
Dutta S.K., Phillips E., Kiddle J.J., Tu C., Silverman D.N.,
Govindasamy L., Agbandje-McKenna M., McKenna R., Tripp B.C.;
"Inhibition of carbonic anhydrase II by thioxolone: a mechanistic and
structural study.";
Biochemistry 47:3174-3184(2008).
[93]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF MUTANTS, MUTAGENESIS OF
ASN-62, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18942852; DOI=10.1021/bi801473w;
Zheng J., Avvaru B.S., Tu C., McKenna R., Silverman D.N.;
"Role of hydrophilic residues in proton transfer during catalysis by
human carbonic anhydrase II.";
Biochemistry 47:12028-12036(2008).
[94]
X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
ENZYME REGULATION.
PubMed=18024029; DOI=10.1016/j.bmcl.2007.10.110;
Guezel O., Temperini C., Innocenti A., Scozzafava A., Salman A.,
Supuran C.T.;
"Carbonic anhydrase inhibitors. Interaction of 2-(hydrazinocarbonyl)-
3-phenyl-1H-indole-5-sulfonamide with 12 mammalian isoforms: kinetic
and X-ray crystallographic studies.";
Bioorg. Med. Chem. Lett. 18:152-158(2008).
[95]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
ENZYME REGULATION.
PubMed=18162396; DOI=10.1016/j.bmcl.2007.12.022;
Temperini C., Cecchi A., Boyle N.A., Scozzafava A., Cabeza J.E.,
Wentworth P. Jr., Blackburn G.M., Supuran C.T.;
"Carbonic anhydrase inhibitors. Interaction of 2-N,N-dimethylamino-
1,3,4-thiadiazole-5-methanesulfonamide with 12 mammalian isoforms:
kinetic and X-ray crystallographic studies.";
Bioorg. Med. Chem. Lett. 18:999-1005(2008).
[96]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
ENZYME REGULATION.
PubMed=18374572; DOI=10.1016/j.bmcl.2008.03.051;
Temperini C., Cecchi A., Scozzafava A., Supuran C.T.;
"Carbonic anhydrase inhibitors. Interaction of indapamide and related
diuretics with 12 mammalian isozymes and X-ray crystallographic
studies for the indapamide-isozyme II adduct.";
Bioorg. Med. Chem. Lett. 18:2567-2573(2008).
[97]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=18359629; DOI=10.1016/j.bmcl.2008.03.023;
Di Fiore A., Pedone C., Antel J., Waldeck H., Witte A., Wurl M.,
Scozzafava A., Supuran C.T., De Simone G.;
"Carbonic anhydrase inhibitors: the X-ray crystal structure of
ethoxzolamide complexed to human isoform II reveals the importance of
thr200 and gln92 for obtaining tight-binding inhibitors.";
Bioorg. Med. Chem. Lett. 18:2669-2674(2008).
[98]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
ENZYME REGULATION.
PubMed=18640037; DOI=10.1016/j.bmcl.2008.06.105;
Temperini C., Innocenti A., Scozzafava A., Supuran C.T.;
"Carbonic anhydrase inhibitors. Interaction of the antitumor sulfamate
EMD 486019 with twelve mammalian carbonic anhydrase isoforms: Kinetic
and X-ray crystallographic studies.";
Bioorg. Med. Chem. Lett. 18:4282-4286(2008).
[99]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH INHIBITORS
INDANESULFONAMIDES.
PubMed=18161740; DOI=10.1002/cmdc.200700274;
D'Ambrosio K., Masereel B., Thiry A., Scozzafava A., Supuran C.T.,
De Simone G.;
"Carbonic anhydrase inhibitors: binding of indanesulfonamides to the
human isoform II.";
ChemMedChem 3:473-477(2008).
[100]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH
(129)XE-CRYPTOPHANE BIOSENSOR.
PubMed=18461940; DOI=10.1021/ja802214x;
Aaron J.A., Chambers J.M., Jude K.M., Di Costanzo L., Dmochowski I.J.,
Christianson D.W.;
"Structure of a (129)Xe-cryptophane biosensor complexed with human
carbonic anhydrase II.";
J. Am. Chem. Soc. 130:6942-6943(2008).
[101]
X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH CO2.
PubMed=18768466; DOI=10.1074/jbc.M805353200;
Domsic J.F., Avvaru B.S., Kim C.U., Gruner S.M., Agbandje-McKenna M.,
Silverman D.N., McKenna R.;
"Entrapment of carbon dioxide in the active site of carbonic anhydrase
II.";
J. Biol. Chem. 283:30766-30771(2008).
[102]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=18260615; DOI=10.1021/jm701319c;
Leese M.P., Jourdan F.L., Gaukroger K., Mahon M.F., Newman S.P.,
Foster P.A., Stengel C., Regis-Lydi S., Ferrandis E., Di Fiore A.,
De Simone G., Supuran C.T., Purohit A., Reed M.J., Potter B.V.;
"Structure-activity relationships of C-17 cyano-substituted
estratrienes as anticancer agents.";
J. Med. Chem. 51:1295-1308(2008).
[103]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
ENZYME REGULATION.
PubMed=18481843; DOI=10.1021/jm800121c;
D'Ambrosio K., Vitale R.-M., Dogne J.-M., Masereel B., Innocenti A.,
Scozzafava A., De Simone G., Supuran C.T.;
"Carbonic anhydrase inhibitors: bioreductive nitro-containing
sulfonamides with selectivity for targeting the tumor associated
isoforms IX and XII.";
J. Med. Chem. 51:3230-3237(2008).
[104]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=18723489; DOI=10.1158/1535-7163.MCT-08-0195;
Woo L.W.L., Fischer D.S., Sharland C.M., Trusselle M., Foster P.A.,
Chander S.K., Di Fiore A., Supuran C.T., De Simone G., Purohit A.,
Reed M.J., Potter B.V.L.;
"Anticancer steroid sulfatase inhibitors: synthesis of a potent
fluorinated second-generation agent, in vitro and in vivo activities,
molecular modeling, and protein crystallography.";
Mol. Cancer Ther. 7:2435-2444(2008).
[105]
X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH INHIBITORS,
ENZYME REGULATION, AND MUTAGENESIS OF ALA-65 AND ASN-67.
PubMed=19170619; DOI=10.1021/bi802035f;
Genis C., Sippel K.H., Case N., Cao W., Avvaru B.S., Tartaglia L.J.,
Govindasamy L., Tu C., Agbandje-McKenna M., Silverman D.N.,
Rosser C.J., McKenna R.;
"Design of a carbonic anhydrase IX active-site mimic to screen
inhibitors for possible anticancer properties.";
Biochemistry 48:1322-1331(2009).
[106]
X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) FREE AND IN COMPLEX WITH ZINC
ION, AND COFACTOR.
PubMed=19583303; DOI=10.1021/bi9007512;
Avvaru B.S., Busby S.A., Chalmers M.J., Griffin P.R.,
Venkatakrishnan B., Agbandje-McKenna M., Silverman D.N., McKenna R.;
"Apo-human carbonic anhydrase II revisited: implications of the loss
of a metal in protein structure, stability, and solvent network.";
Biochemistry 48:7365-7372(2009).
[107]
X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 1-260 IN COMPLEX WITH
INHIBITOR THIABENDAZOLE-5-SULFONAMIDE, AND ENZYME REGULATION.
PubMed=19186056; DOI=10.1016/j.bmcl.2009.01.038;
Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A.,
Muehlschlegel F.A., Supuran C.T.;
"A thiabendazole sulfonamide shows potent inhibitory activity against
mammalian and nematode alpha-carbonic anhydrases.";
Bioorg. Med. Chem. Lett. 19:1371-1375(2009).
[108]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-260 IN COMPLEX WITH
COUMARIN INHIBITORS, AND ENZYME REGULATION.
PubMed=19206230; DOI=10.1021/ja809683v;
Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A.,
Scozzafava A., Quinn R.J., Supuran C.T.;
"Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a
new class of suicide inhibitors.";
J. Am. Chem. Soc. 131:3057-3062(2009).
[109]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=19115843; DOI=10.1021/jm801386n;
Temperini C., Cecchi A., Scozzafava A., Supuran C.T.;
"Carbonic anhydrase inhibitors. Comparison of chlorthalidone and
indapamide X-ray crystal structures in adducts with isozyme II: when
three water molecules and the keto-enol tautomerism make the
difference.";
J. Med. Chem. 52:322-328(2009).
[110]
X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=19731956; DOI=10.1021/jm900641r;
Vitale R.M., Alterio V., Innocenti A., Winum J.-Y., Monti S.M.,
De Simone G., Supuran C.T.;
"Carbonic anhydrase inhibitors. Comparison of aliphatic sulfamate/bis-
sulfamate adducts with isozymes II and IX as a platform for designing
tight-binding, more isoform-selective inhibitors.";
J. Med. Chem. 52:5990-5998(2009).
[111]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-260 IN COMPLEX WITH
INHIBITORS.
PubMed=19827837; DOI=10.1021/jm900914e;
Lopez M., Paul B., Hofmann A., Morizzi J., Wu Q.K., Charman S.A.,
Innocenti A., Vullo D., Supuran C.T., Poulsen S.-A.;
"S-glycosyl primary sulfonamides--a new structural class for selective
inhibition of cancer-associated carbonic anhydrases.";
J. Med. Chem. 52:6421-6432(2009).
[112]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-260 IN COMPLEX WITH
INHIBITORS, AND ENZYME REGULATION.
PubMed=19778001; DOI=10.1021/jp906593c;
Ciani L., Cecchi A., Temperini C., Supuran C.T., Ristori S.;
"Dissecting the inhibition mechanism of cytosolic versus transmembrane
carbonic anhydrases by ESR.";
J. Phys. Chem. B 113:13998-14005(2009).
[113]
X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, AND
ENZYME REGULATION.
PubMed=19520834; DOI=10.1073/pnas.0904184106;
Sjoeblom B., Polentarutti M., Djinovic-Carugo K.;
"Structural study of X-ray induced activation of carbonic anhydrase.";
Proc. Natl. Acad. Sci. U.S.A. 106:10609-10613(2009).
[114]
VARIANT JOGJAKARTA GLU-18.
PubMed=6817747; DOI=10.1007/BF00484072;
Jones G.L., Sofro A.S.M., Shaw D.C.;
"Chemical and enzymological characterization of an Indonesian variant
of human erythrocyte carbonic anhydrase II, CAII Jogjakarta (17 Lys
leads to Glu).";
Biochem. Genet. 20:979-1000(1982).
[115]
VARIANT MELBOURNE HIS-236.
PubMed=6407977; DOI=10.1007/BF00274768;
Jones G.L., Shaw D.C.;
"A chemical and enzymological comparison of the common major human
erythrocyte carbonic anhydrase II, its minor component, and a new
genetic variant, CA II Melbourne (237 Pro leads to His).";
Hum. Genet. 63:392-399(1983).
[116]
VARIANT OPTB3 TYR-107.
PubMed=1928091;
Venta P.J., Welty R.J., Johnson T.M., Sly W.S., Tashian R.E.;
"Carbonic anhydrase II deficiency syndrome in a Belgian family is
caused by a point mutation at an invariant histidine residue (107
His-->Tyr): complete structure of the normal human CA II gene.";
Am. J. Hum. Genet. 49:1082-1090(1991).
[117]
VARIANT OPTB3 TYR-107.
PubMed=1542674; DOI=10.1073/pnas.89.5.1804;
Roth D.E., Venta P.J., Tashian R.E., Sly W.S.;
"Molecular basis of human carbonic anhydrase II deficiency.";
Proc. Natl. Acad. Sci. U.S.A. 89:1804-1808(1992).
[118]
VARIANT OPTB3 TYR-107.
PubMed=8834238; DOI=10.1007/BF02267062;
Soda H., Yukizane S., Yoshida I., Koga Y., Aramaki S., Kato H.;
"A point mutation in exon 3 (His 107-->Tyr) in two unrelated Japanese
patients with carbonic anhydrase II deficiency with central nervous
system involvement.";
Hum. Genet. 97:435-437(1996).
[119]
VARIANT OPTB3 PRO-92.
PubMed=9143915;
DOI=10.1002/(SICI)1098-1004(1997)9:5<383::AID-HUMU1>3.3.CO;2-K;
Hu P.Y., Lim E.J., Ciccolella J., Strisciuglio P., Sly W.S.;
"Seven novel mutations in carbonic anhydrase II deficiency syndrome
identified by SSCP and direct sequencing analysis.";
Hum. Mutat. 9:383-387(1997).
[120]
VARIANTS OPTB3 PRO-92; TYR-94; TYR-107 AND ARG-144, AND
CHARACTERIZATION OF VARIANTS TYR-94 AND ARG-144.
PubMed=15300855; DOI=10.1002/humu.9266;
Shah G.N., Bonapace G., Hu P.Y., Strisciuglio P., Sly W.S.;
"Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal
tubular acidosis and brain calcification): novel mutations in CA2
identified by direct sequencing expand the opportunity for genotype-
phenotype correlation.";
Hum. Mutat. 24:272-272(2004).
-!- FUNCTION: Essential for bone resorption and osteoclast
differentiation (By similarity). Reversible hydration of carbon
dioxide. Can hydrate cyanamide to urea. Involved in the regulation
of fluid secretion into the anterior chamber of the eye.
Contributes to intracellular pH regulation in the duodenal upper
villous epithelium during proton-coupled peptide absorption.
Stimulates the chloride-bicarbonate exchange activity of SLC26A6.
{ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:11831900,
ECO:0000269|PubMed:15990874, ECO:0007001}.
-!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:11076507,
ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460,
ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891,
ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019,
ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440,
ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850,
ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159,
ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242,
ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494,
ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308,
ECO:0000269|PubMed:9865942};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:19583303};
Note=Zinc. Can also use cobalt(II) with lower efficiency, but not
copper(II), nickel(II) and manganese(II).
{ECO:0000269|PubMed:19583303};
-!- ENZYME REGULATION: Activated by X-ray, histamine, L-adrenaline,
L- and D-phenylalanine, L- and D-histidine, L-His-OMe and beta-
Ala-His (carnosine). Competitively inhibited by saccharin,
thioxolone, coumarins, 667-coumate, celecoxib (Celebrex),
valdecoxib (Bextra), SC-125, SC-560, diclofenac, acetate, azide,
bromide, sulfonamide derivatives such as acetazolamide (AZA),
methazolamide (MZA), ethoxzolamide (EZA), dichlorophenamide (DCP),
brinzolamide, dansylamide, thiabendazole-5-sulfonamide,
trifluoromethane sulfonamide and N-hydroxysulfamide, fructose-
based sugar sulfamate RWJ-37497, and Foscarnet (phosphonoformate
trisodium salt). Repressed strongly by hydrogen sulfide(HS) and
weakly by nitrate (NO(3)). Esterase activity weakly reduced by
cyanamide. N-hydroxyurea interfers with zinc binding and inhibit
activity. {ECO:0000269|PubMed:11802772,
ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:14736236,
ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:16290146,
ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16759856,
ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057,
ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17540563,
ECO:0000269|PubMed:17588751, ECO:0000269|PubMed:17705204,
ECO:0000269|PubMed:18024029, ECO:0000269|PubMed:18162396,
ECO:0000269|PubMed:18266323, ECO:0000269|PubMed:18374572,
ECO:0000269|PubMed:18481843, ECO:0000269|PubMed:18618712,
ECO:0000269|PubMed:18640037, ECO:0000269|PubMed:1910042,
ECO:0000269|PubMed:19170619, ECO:0000269|PubMed:19186056,
ECO:0000269|PubMed:19206230, ECO:0000269|PubMed:19520834,
ECO:0000269|PubMed:19778001, ECO:0000269|PubMed:9265618}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=550 nm {ECO:0000269|PubMed:10550681,
ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:18942852,
ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:1910042,
ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:9398308};
Note=At pH 7.0. Shows a second maximum at 618 nm.;
Kinetic parameters:
KM=10 mM for CO(2) {ECO:0000269|PubMed:10550681,
ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:18942852,
ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:1910042,
ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:9398308};
KM=82 mM for H(2)CO(3) {ECO:0000269|PubMed:10550681,
ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:18942852,
ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:1910042,
ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:9398308};
KM=3 mM for 4-nitrophenyl acetate {ECO:0000269|PubMed:10550681,
ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:18942852,
ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:1910042,
ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:9398308};
pH dependence:
Optimum pH is 6-8. {ECO:0000269|PubMed:10550681,
ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:18942852,
ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:1910042,
ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:9398308};
-!- SUBUNIT: Interacts with SLC4A4. Interaction with SLC4A7 regulates
SLC4A7 transporter activity. Interacts with SLC26A6 isoform 4 (via
C-terminus cytoplasmic domain). {ECO:0000269|PubMed:10550681,
ECO:0000269|PubMed:11015219, ECO:0000269|PubMed:11076507,
ECO:0000269|PubMed:11327835, ECO:0000269|PubMed:11572683,
ECO:0000269|PubMed:11802772, ECO:0000269|PubMed:11818565,
ECO:0000269|PubMed:11831900, ECO:0000269|PubMed:12056894,
ECO:0000269|PubMed:12166932, ECO:0000269|PubMed:12499545,
ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293,
ECO:0000269|PubMed:14567693, ECO:0000269|PubMed:14736236,
ECO:0000269|PubMed:14736710, ECO:0000269|PubMed:1474587,
ECO:0000269|PubMed:15218065, ECO:0000269|PubMed:15299481,
ECO:0000269|PubMed:15299482, ECO:0000269|PubMed:15453828,
ECO:0000269|PubMed:15865431, ECO:0000269|PubMed:15990874,
ECO:0000269|PubMed:16134940, ECO:0000269|PubMed:16214338,
ECO:0000269|PubMed:16290146, ECO:0000269|PubMed:16506782,
ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16759856,
ECO:0000269|PubMed:16787097, ECO:0000269|PubMed:16807956,
ECO:0000269|PubMed:16820676, ECO:0000269|PubMed:16942027,
ECO:0000269|PubMed:17000110, ECO:0000269|PubMed:17071654,
ECO:0000269|PubMed:17125255, ECO:0000269|PubMed:17127057,
ECO:0000269|PubMed:17181151, ECO:0000269|PubMed:17251017,
ECO:0000269|PubMed:17346964, ECO:0000269|PubMed:17407288,
ECO:0000269|PubMed:17540563, ECO:0000269|PubMed:17588751,
ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:18024029,
ECO:0000269|PubMed:18161740, ECO:0000269|PubMed:18162396,
ECO:0000269|PubMed:18260615, ECO:0000269|PubMed:18266323,
ECO:0000269|PubMed:18359629, ECO:0000269|PubMed:18374572,
ECO:0000269|PubMed:18461940, ECO:0000269|PubMed:18481843,
ECO:0000269|PubMed:18640037, ECO:0000269|PubMed:18723489,
ECO:0000269|PubMed:18768466, ECO:0000269|PubMed:1909891,
ECO:0000269|PubMed:19115843, ECO:0000269|PubMed:19170619,
ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230,
ECO:0000269|PubMed:1932029, ECO:0000269|PubMed:19520834,
ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:19731956,
ECO:0000269|PubMed:19778001, ECO:0000269|PubMed:19827837,
ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020,
ECO:0000269|PubMed:7608893, ECO:0000269|PubMed:7696263,
ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386,
ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8070585,
ECO:0000269|PubMed:8142888, ECO:0000269|PubMed:8218160,
ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673,
ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430,
ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389,
ECO:0000269|PubMed:8557623, ECO:0000269|PubMed:8639494,
ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9265618,
ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9541386,
ECO:0000269|PubMed:9865942}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15990874}.
Cell membrane {ECO:0000269|PubMed:15990874}. Note=Colocalized with
SLC26A6 at the surface of the cell membrane in order to form a
bicarbonate transport metabolon. Displaced from the cytosolic
surface of the cell membrane by PKC in phorbol myristate acetate
(PMA)-induced cells.
-!- DISEASE: Osteopetrosis, autosomal recessive 3 (OPTB3)
[MIM:259730]: A rare genetic disease characterized by abnormally
dense bone, due to defective resorption of immature bone.
Osteopetrosis occurs in two forms: a severe autosomal recessive
form occurring in utero, infancy, or childhood, and a benign
autosomal dominant form occurring in adolescence or adulthood.
Recessive osteopetrosis commonly manifests in early infancy with
macrocephaly, feeding difficulties, evolving blindness and
deafness, bone marrow failure, severe anemia, and
hepatosplenomegaly. Deafness and blindness are generally thought
to represent effects of pressure on nerves. OPTB3 is associated
with renal tubular acidosis, cerebral calcification (marble brain
disease) and in some cases with mental retardation.
{ECO:0000269|PubMed:15300855, ECO:0000269|PubMed:1542674,
ECO:0000269|PubMed:1928091, ECO:0000269|PubMed:8834238,
ECO:0000269|PubMed:9143915}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Target of drugs used in treatments against glaucoma
disorder and breast cancer.
-!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
{ECO:0000320}.
-----------------------------------------------------------------------
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EMBL; M77181; AAA51909.1; -; Genomic_DNA.
EMBL; M77176; AAA51909.1; JOINED; Genomic_DNA.
EMBL; M77177; AAA51909.1; JOINED; Genomic_DNA.
EMBL; M77178; AAA51909.1; JOINED; Genomic_DNA.
EMBL; M77179; AAA51909.1; JOINED; Genomic_DNA.
EMBL; M77180; AAA51909.1; JOINED; Genomic_DNA.
EMBL; Y00339; CAA68426.1; -; mRNA.
EMBL; X03251; CAA27012.1; -; Genomic_DNA.
EMBL; J03037; AAA51908.1; -; mRNA.
EMBL; CR536526; CAG38763.1; -; mRNA.
EMBL; CR541875; CAG46673.1; -; mRNA.
EMBL; AK312978; BAG35815.1; -; mRNA.
EMBL; CH471068; EAW87136.1; -; Genomic_DNA.
EMBL; BC011949; AAH11949.1; -; mRNA.
EMBL; M36532; AAA51911.1; -; mRNA.
CCDS; CCDS6239.1; -.
PIR; A27175; CRHU2.
RefSeq; NP_000058.1; NM_000067.2.
UniGene; Hs.155097; -.
PDB; 12CA; X-ray; 2.40 A; A=1-260.
PDB; 1A42; X-ray; 2.25 A; A=2-260.
PDB; 1AM6; X-ray; 2.00 A; A=2-260.
PDB; 1AVN; X-ray; 2.00 A; A=2-260.
PDB; 1BCD; X-ray; 1.90 A; A=2-260.
PDB; 1BIC; X-ray; 1.90 A; A=2-260.
PDB; 1BN1; X-ray; 2.10 A; A=2-260.
PDB; 1BN3; X-ray; 2.20 A; A=2-260.
PDB; 1BN4; X-ray; 2.10 A; A=2-260.
PDB; 1BNM; X-ray; 2.60 A; A=2-260.
PDB; 1BNN; X-ray; 2.30 A; A=2-260.
PDB; 1BNQ; X-ray; 2.40 A; A=2-260.
PDB; 1BNT; X-ray; 2.15 A; A=2-260.
PDB; 1BNU; X-ray; 2.15 A; A=2-260.
PDB; 1BNV; X-ray; 2.40 A; A=2-260.
PDB; 1BNW; X-ray; 2.25 A; A=2-260.
PDB; 1BV3; X-ray; 1.85 A; A=2-260.
PDB; 1CA2; X-ray; 2.00 A; A=2-260.
PDB; 1CA3; X-ray; 2.30 A; A=1-260.
PDB; 1CAH; X-ray; 1.88 A; A=2-260.
PDB; 1CAI; X-ray; 1.80 A; A=2-260.
PDB; 1CAJ; X-ray; 1.90 A; A=2-260.
PDB; 1CAK; X-ray; 1.90 A; A=2-260.
PDB; 1CAL; X-ray; 2.20 A; A=2-260.
PDB; 1CAM; X-ray; 1.70 A; A=2-260.
PDB; 1CAN; X-ray; 1.90 A; A=2-260.
PDB; 1CAO; X-ray; 1.90 A; A=2-260.
PDB; 1CAY; X-ray; 2.10 A; A=2-260.
PDB; 1CAZ; X-ray; 1.90 A; A=2-260.
PDB; 1CCS; X-ray; 2.35 A; A=2-260.
PDB; 1CCT; X-ray; 2.20 A; A=2-260.
PDB; 1CCU; X-ray; 2.25 A; A=2-260.
PDB; 1CIL; X-ray; 1.60 A; A=2-260.
PDB; 1CIM; X-ray; 2.10 A; A=2-260.
PDB; 1CIN; X-ray; 2.10 A; A=2-260.
PDB; 1CNB; X-ray; 2.35 A; A=2-260.
PDB; 1CNC; X-ray; 2.20 A; A=2-260.
PDB; 1CNG; X-ray; 1.90 A; A=2-260.
PDB; 1CNH; X-ray; 2.05 A; A=2-260.
PDB; 1CNI; X-ray; 1.80 A; A=2-260.
PDB; 1CNJ; X-ray; 1.80 A; A=2-260.
PDB; 1CNK; X-ray; 2.15 A; A=2-260.
PDB; 1CNW; X-ray; 2.00 A; A=1-260.
PDB; 1CNX; X-ray; 1.90 A; A=1-260.
PDB; 1CNY; X-ray; 2.30 A; A=1-260.
PDB; 1CRA; X-ray; 1.90 A; A=2-260.
PDB; 1CVA; X-ray; 2.25 A; A=2-260.
PDB; 1CVB; X-ray; 2.40 A; A=2-260.
PDB; 1CVC; X-ray; 2.30 A; A=2-260.
PDB; 1CVD; X-ray; 2.20 A; A=5-259.
PDB; 1CVE; X-ray; 2.25 A; A=2-260.
PDB; 1CVF; X-ray; 2.25 A; A=2-260.
PDB; 1CVH; X-ray; 2.30 A; A=5-259.
PDB; 1DCA; X-ray; 2.20 A; A=1-260.
PDB; 1DCB; X-ray; 2.10 A; A=1-260.
PDB; 1EOU; X-ray; 2.10 A; A=1-260.
PDB; 1F2W; X-ray; 1.90 A; A=2-260.
PDB; 1FQL; X-ray; 2.00 A; A=1-260.
PDB; 1FQM; X-ray; 2.00 A; A=1-260.
PDB; 1FQN; X-ray; 2.00 A; A=1-260.
PDB; 1FQR; X-ray; 2.00 A; A=1-260.
PDB; 1FR4; X-ray; 1.60 A; A=1-260.
PDB; 1FR7; X-ray; 1.50 A; A/B=1-260.
PDB; 1FSN; X-ray; 2.00 A; A/B=1-260.
PDB; 1FSQ; X-ray; 2.00 A; A/B=1-260.
PDB; 1FSR; X-ray; 2.00 A; A/B=1-260.
PDB; 1G0E; X-ray; 1.60 A; A=1-260.
PDB; 1G0F; X-ray; 1.60 A; A=1-260.
PDB; 1G1D; X-ray; 2.04 A; A=2-260.
PDB; 1G3Z; X-ray; 1.86 A; A=2-260.
PDB; 1G45; X-ray; 1.83 A; A=2-260.
PDB; 1G46; X-ray; 1.84 A; A=2-260.
PDB; 1G48; X-ray; 1.86 A; A=2-260.
PDB; 1G4J; X-ray; 1.84 A; A=2-260.
PDB; 1G4O; X-ray; 1.96 A; A=2-260.
PDB; 1G52; X-ray; 1.80 A; A=2-260.
PDB; 1G53; X-ray; 1.94 A; A=2-260.
PDB; 1G54; X-ray; 1.86 A; A=2-260.
PDB; 1H4N; X-ray; 2.00 A; A=2-260.
PDB; 1H9N; X-ray; 1.85 A; A=2-260.
PDB; 1H9Q; X-ray; 2.20 A; A=2-260.
PDB; 1HCA; X-ray; 2.30 A; A=1-260.
PDB; 1HEA; X-ray; 2.00 A; A=1-260.
PDB; 1HEB; X-ray; 2.00 A; A=1-260.
PDB; 1HEC; X-ray; 2.00 A; A=1-260.
PDB; 1HED; X-ray; 2.00 A; A=1-260.
PDB; 1HVA; X-ray; 2.30 A; A=1-260.
PDB; 1I8Z; X-ray; 1.93 A; A=2-260.
PDB; 1I90; X-ray; 2.00 A; A=2-260.
PDB; 1I91; X-ray; 2.00 A; A=2-260.
PDB; 1I9L; X-ray; 1.93 A; A=2-260.
PDB; 1I9M; X-ray; 1.84 A; A=2-260.
PDB; 1I9N; X-ray; 1.86 A; A=2-260.
PDB; 1I9O; X-ray; 1.86 A; A=2-260.
PDB; 1I9P; X-ray; 1.92 A; A=2-260.
PDB; 1I9Q; X-ray; 1.80 A; A=2-260.
PDB; 1IF4; X-ray; 1.93 A; A=2-260.
PDB; 1IF5; X-ray; 2.00 A; A=2-260.
PDB; 1IF6; X-ray; 2.09 A; A=2-259.
PDB; 1IF7; X-ray; 1.98 A; A=2-260.
PDB; 1IF8; X-ray; 1.94 A; A=2-260.
PDB; 1IF9; X-ray; 2.00 A; A=2-260.
PDB; 1KWQ; X-ray; 2.60 A; A=1-260.
PDB; 1KWR; X-ray; 2.25 A; A=1-260.
PDB; 1LG5; X-ray; 1.75 A; A=1-260.
PDB; 1LG6; X-ray; 2.20 A; A=1-260.
PDB; 1LGD; X-ray; 1.90 A; A=1-260.
PDB; 1LUG; X-ray; 0.95 A; A=2-260.
PDB; 1LZV; X-ray; 2.30 A; A=1-260.
PDB; 1MOO; X-ray; 1.05 A; A=1-260.
PDB; 1MUA; X-ray; 1.70 A; A=4-259.
PDB; 1OKL; X-ray; 2.10 A; A=2-260.
PDB; 1OKM; X-ray; 2.20 A; A=2-260.
PDB; 1OKN; X-ray; 2.40 A; A=2-260.
PDB; 1OQ5; X-ray; 1.50 A; A=2-259.
PDB; 1RAY; X-ray; 1.80 A; A=2-260.
PDB; 1RAZ; X-ray; 1.90 A; A=2-260.
PDB; 1RZA; X-ray; 1.90 A; A=2-260.
PDB; 1RZB; X-ray; 1.80 A; A=2-260.
PDB; 1RZC; X-ray; 1.90 A; A=2-260.
PDB; 1RZD; X-ray; 1.90 A; A=2-260.
PDB; 1RZE; X-ray; 1.90 A; A=2-260.
PDB; 1T9N; X-ray; 2.00 A; A=1-259.
PDB; 1TB0; X-ray; 2.00 A; X=1-259.
PDB; 1TBT; X-ray; 2.00 A; X=1-259.
PDB; 1TE3; X-ray; 2.00 A; X=1-260.
PDB; 1TEQ; X-ray; 2.00 A; X=1-260.
PDB; 1TEU; X-ray; 2.00 A; X=1-260.
PDB; 1TG3; X-ray; 1.80 A; A=1-260.
PDB; 1TG9; X-ray; 1.90 A; A=1-260.
PDB; 1TH9; X-ray; 1.63 A; A=1-260.
PDB; 1THK; X-ray; 1.80 A; A=1-260.
PDB; 1TTM; X-ray; 1.95 A; A=2-259.
PDB; 1UGA; X-ray; 2.00 A; A=3-260.
PDB; 1UGB; X-ray; 2.00 A; A=3-260.
PDB; 1UGC; X-ray; 2.00 A; A=3-260.
PDB; 1UGD; X-ray; 2.00 A; A=3-260.
PDB; 1UGE; X-ray; 1.90 A; A=3-260.
PDB; 1UGF; X-ray; 2.00 A; A=3-260.
PDB; 1UGG; X-ray; 2.20 A; A=3-260.
PDB; 1XEG; X-ray; 1.81 A; A=1-260.
PDB; 1XEV; X-ray; 2.20 A; A/B/C/D=1-260.
PDB; 1XPZ; X-ray; 2.02 A; A=3-260.
PDB; 1XQ0; X-ray; 1.76 A; A=2-260.
PDB; 1YDA; X-ray; 2.10 A; A=2-260.
PDB; 1YDB; X-ray; 1.90 A; A=2-260.
PDB; 1YDC; X-ray; 1.95 A; A=2-260.
PDB; 1YDD; X-ray; 2.10 A; A=2-260.
PDB; 1YO0; X-ray; 1.80 A; A=1-260.
PDB; 1YO1; X-ray; 1.70 A; A=1-260.
PDB; 1YO2; X-ray; 1.80 A; A=1-259.
PDB; 1Z9Y; X-ray; 1.66 A; A=2-259.
PDB; 1ZE8; X-ray; 2.00 A; A=2-260.
PDB; 1ZFK; X-ray; 1.56 A; A=2-259.
PDB; 1ZFQ; X-ray; 1.55 A; A=2-259.
PDB; 1ZGE; X-ray; 1.65 A; A=2-259.
PDB; 1ZGF; X-ray; 1.75 A; A=2-259.
PDB; 1ZH9; X-ray; 1.70 A; A=2-259.
PDB; 1ZSA; X-ray; 2.50 A; A=2-260.
PDB; 1ZSB; X-ray; 2.00 A; A=2-260.
PDB; 1ZSC; X-ray; 1.80 A; A=2-260.
PDB; 2ABE; X-ray; 2.00 A; A=2-259.
PDB; 2AW1; X-ray; 1.46 A; A=2-260.
PDB; 2AX2; X-ray; 1.50 A; A=1-259.
PDB; 2CA2; X-ray; 1.90 A; A=2-260.
PDB; 2CBA; X-ray; 1.54 A; A=2-260.
PDB; 2CBB; X-ray; 1.67 A; A=2-260.
PDB; 2CBC; X-ray; 1.88 A; A=2-260.
PDB; 2CBD; X-ray; 1.67 A; A=2-260.
PDB; 2CBE; X-ray; 1.82 A; A=2-260.
PDB; 2EU2; X-ray; 1.15 A; A=1-260.
PDB; 2EU3; X-ray; 1.60 A; A=1-260.
PDB; 2EZ7; X-ray; 2.00 A; A=1-259.
PDB; 2F14; X-ray; 1.71 A; A=2-259.
PDB; 2FMG; X-ray; 1.60 A; A=1-259.
PDB; 2FMZ; X-ray; 1.60 A; A=1-259.
PDB; 2FNK; X-ray; 1.80 A; A=1-260.
PDB; 2FNM; X-ray; 1.80 A; A=1-260.
PDB; 2FNN; X-ray; 1.80 A; A=1-260.
PDB; 2FOQ; X-ray; 1.25 A; A=1-259.
PDB; 2FOS; X-ray; 1.10 A; A=1-259.
PDB; 2FOU; X-ray; 0.99 A; A=1-259.
PDB; 2FOV; X-ray; 1.15 A; A=1-259.
PDB; 2GD8; X-ray; 1.46 A; A=2-259.
PDB; 2GEH; X-ray; 2.00 A; A=1-259.
PDB; 2H15; X-ray; 1.90 A; A=1-259.
PDB; 2H4N; X-ray; 1.90 A; A=2-260.
PDB; 2HD6; X-ray; 1.80 A; A=2-259.
PDB; 2HKK; X-ray; 1.90 A; A=1-260.
PDB; 2HL4; X-ray; 1.55 A; A=2-260.
PDB; 2HNC; X-ray; 1.55 A; A=2-259.
PDB; 2HOC; X-ray; 2.10 A; A=2-259.
PDB; 2ILI; X-ray; 1.05 A; A=2-259.
PDB; 2NNG; X-ray; 1.20 A; A=2-260.
PDB; 2NNO; X-ray; 1.01 A; A=2-260.
PDB; 2NNS; X-ray; 1.03 A; A=2-260.
PDB; 2NNV; X-ray; 1.10 A; A=2-260.
PDB; 2NWO; X-ray; 1.70 A; A=1-259.
PDB; 2NWP; X-ray; 1.80 A; A=1-259.
PDB; 2NWY; X-ray; 1.65 A; A=1-259.
PDB; 2NWZ; X-ray; 1.80 A; A=1-259.
PDB; 2NXR; X-ray; 1.70 A; A=1-259.
PDB; 2NXS; X-ray; 1.80 A; A=1-259.
PDB; 2NXT; X-ray; 1.15 A; A=1-260.
PDB; 2O4Z; X-ray; 2.10 A; A=1-260.
PDB; 2OSF; X-ray; 1.60 A; A=2-260.
PDB; 2OSM; X-ray; 1.60 A; A=2-260.
PDB; 2POU; X-ray; 1.60 A; A=1-259.
PDB; 2POV; X-ray; 1.60 A; A=1-258.
PDB; 2POW; X-ray; 1.75 A; A=1-259.
PDB; 2Q1B; X-ray; 1.70 A; A=1-260.
PDB; 2Q1Q; X-ray; 1.90 A; A=1-260.
PDB; 2Q38; X-ray; 1.95 A; A=1-260.
PDB; 2QO8; X-ray; 1.40 A; A=2-260.
PDB; 2QOA; X-ray; 1.60 A; A=2-260.
PDB; 2QP6; X-ray; 1.45 A; A=2-260.
PDB; 2VVA; X-ray; 1.56 A; X=1-260.
PDB; 2VVB; X-ray; 1.66 A; X=1-260.
PDB; 2WD2; X-ray; 1.49 A; A=2-259.
PDB; 2WD3; X-ray; 1.80 A; A=2-260.
PDB; 2WEG; X-ray; 1.10 A; A=2-260.
PDB; 2WEH; X-ray; 2.09 A; A=2-260.
PDB; 2WEJ; X-ray; 1.45 A; A=2-260.
PDB; 2WEO; X-ray; 1.40 A; A=2-260.
PDB; 2X7S; X-ray; 1.64 A; A=2-260.
PDB; 2X7T; X-ray; 1.89 A; A=2-260.
PDB; 2X7U; X-ray; 2.12 A; A=2-260.
PDB; 3B4F; X-ray; 1.89 A; A=1-260.
PDB; 3BET; X-ray; 1.85 A; A=2-260.
PDB; 3BL0; X-ray; 1.90 A; A=1-260.
PDB; 3BL1; X-ray; 2.10 A; A=1-260.
PDB; 3C7P; X-ray; 1.70 A; A=1-260.
PDB; 3CA2; X-ray; 2.00 A; A=2-260.
PDB; 3CAJ; X-ray; 1.80 A; A=1-260.
PDB; 3CYU; X-ray; 1.70 A; A=1-260.
PDB; 3D8W; X-ray; 1.70 A; A=1-260.
PDB; 3D92; X-ray; 1.10 A; A=1-260.
PDB; 3D93; X-ray; 1.10 A; A=1-260.
PDB; 3D9Z; X-ray; 1.65 A; A=1-260.
PDB; 3DAZ; X-ray; 1.60 A; A=1-260.
PDB; 3DBU; X-ray; 1.70 A; A=1-260.
PDB; 3DC3; X-ray; 1.70 A; A=1-260.
PDB; 3DC9; X-ray; 1.60 A; A=1-260.
PDB; 3DCC; X-ray; 1.60 A; A=1-260.
PDB; 3DCS; X-ray; 1.80 A; A=1-260.
PDB; 3DCW; X-ray; 1.50 A; A=1-260.
PDB; 3DD0; X-ray; 1.48 A; A=1-260.
PDB; 3DD8; X-ray; 1.90 A; A=1-260.
PDB; 3DV7; X-ray; 1.70 A; A=2-260.
PDB; 3DVB; X-ray; 1.70 A; A=2-260.
PDB; 3DVC; X-ray; 1.60 A; A=2-260.
PDB; 3DVD; X-ray; 1.60 A; A=2-260.
PDB; 3EFI; X-ray; 1.75 A; A=2-260.
PDB; 3EFT; X-ray; 1.85 A; A=1-260.
PDB; 3F4X; X-ray; 1.90 A; A=1-260.
PDB; 3F8E; X-ray; 2.00 A; A=1-260.
PDB; 3FFP; X-ray; 1.81 A; X=1-260.
PDB; 3GZ0; X-ray; 1.26 A; A=2-260.
PDB; 3HFP; X-ray; 2.10 A; A=1-260.
PDB; 3HKN; X-ray; 1.80 A; A=1-260.
PDB; 3HKQ; X-ray; 1.70 A; A=1-260.
PDB; 3HKT; X-ray; 2.36 A; A=1-260.
PDB; 3HKU; X-ray; 1.80 A; A=1-260.
PDB; 3HLJ; X-ray; 1.44 A; A=1-260.
PDB; 3HS4; X-ray; 1.10 A; A=1-260.
PDB; 3IBI; X-ray; 1.93 A; A=2-260.
PDB; 3IBL; X-ray; 1.55 A; A=2-260.
PDB; 3IBN; X-ray; 2.20 A; A=2-260.
PDB; 3IBU; X-ray; 1.41 A; A=2-260.
PDB; 3IEO; X-ray; 2.00 A; A=1-260.
PDB; 3IGP; X-ray; 1.65 A; A=1-260.
PDB; 3K2F; X-ray; 1.98 A; A=1-260.
PDB; 3K34; X-ray; 0.90 A; A=1-260.
PDB; 3K7K; X-ray; 1.90 A; A=1-260.
PDB; 3KIG; X-ray; 1.39 A; A=1-260.
PDB; 3KKX; Neutron; 2.00 A; A=1-260.
PDB; 3KNE; X-ray; 1.35 A; A=1-260.
PDB; 3KOI; X-ray; 1.64 A; A=1-260.
PDB; 3KOK; X-ray; 1.50 A; A=1-260.
PDB; 3KON; X-ray; 1.50 A; A=1-260.
PDB; 3KS3; X-ray; 0.90 A; A=1-260.
PDB; 3KWA; X-ray; 2.00 A; A=1-260.
PDB; 3L14; X-ray; 1.22 A; A=1-260.
PDB; 3M04; X-ray; 1.40 A; A=1-260.
PDB; 3M14; X-ray; 1.38 A; A=1-260.
PDB; 3M1J; X-ray; 1.80 A; A=1-260.
PDB; 3M1K; X-ray; 1.35 A; A=1-260.
PDB; 3M1Q; X-ray; 1.69 A; A=1-260.
PDB; 3M1W; X-ray; 1.38 A; A=1-260.
PDB; 3M2N; X-ray; 1.65 A; A=1-260.
PDB; 3M2X; X-ray; 1.87 A; A=1-260.
PDB; 3M2Y; X-ray; 1.17 A; A=1-260.
PDB; 3M2Z; X-ray; 1.70 A; A=1-260.
PDB; 3M3X; X-ray; 1.68 A; A=1-260.
PDB; 3M40; X-ray; 1.60 A; A=1-260.
PDB; 3M5E; X-ray; 1.70 A; A=1-260.
PDB; 3M5S; X-ray; 1.40 A; A=1-260.
PDB; 3M5T; X-ray; 1.95 A; A=1-260.
PDB; 3M67; X-ray; 1.80 A; A=1-260.
PDB; 3M96; X-ray; 1.40 A; A=1-260.
PDB; 3M98; X-ray; 1.50 A; A=1-260.
PDB; 3MHC; X-ray; 1.70 A; A=1-260.
PDB; 3MHI; X-ray; 1.70 A; A=1-260.
PDB; 3MHL; X-ray; 1.90 A; A=1-260.
PDB; 3MHM; X-ray; 1.50 A; A=1-260.
PDB; 3MHO; X-ray; 1.15 A; A=1-260.
PDB; 3ML2; X-ray; 1.80 A; A=1-260.
PDB; 3MMF; X-ray; 1.50 A; A=1-260.
PDB; 3MNA; X-ray; 1.50 A; A=1-260.
PDB; 3MNH; X-ray; 1.65 A; A=1-260.
PDB; 3MNI; X-ray; 1.75 A; A=1-260.
PDB; 3MNJ; X-ray; 1.75 A; A=1-260.
PDB; 3MNK; X-ray; 1.75 A; A=1-260.
PDB; 3MNU; X-ray; 1.80 A; A=2-260.
PDB; 3MWO; X-ray; 1.40 A; A/B=1-260.
PDB; 3MYQ; X-ray; 1.35 A; A=1-260.
PDB; 3MZC; X-ray; 1.50 A; A=1-260.
PDB; 3N0N; X-ray; 1.50 A; A=1-260.
PDB; 3N2P; X-ray; 1.65 A; A=1-260.
PDB; 3N3J; X-ray; 1.50 A; A=1-260.
PDB; 3N4B; X-ray; 1.60 A; A=1-260.
PDB; 3NB5; X-ray; 1.80 A; A=1-260.
PDB; 3NI5; X-ray; 2.10 A; A=1-260.
PDB; 3NJ9; X-ray; 2.00 A; A=1-260.
PDB; 3OIK; X-ray; 1.50 A; A=1-260.
PDB; 3OIL; X-ray; 1.50 A; A=1-260.
PDB; 3OIM; X-ray; 1.45 A; A=1-260.
PDB; 3OKU; X-ray; 1.45 A; A=1-260.
PDB; 3OKV; X-ray; 1.45 A; A=1-260.
PDB; 3OY0; X-ray; 1.60 A; A=1-260.
PDB; 3OYQ; X-ray; 1.47 A; A=1-260.
PDB; 3OYS; X-ray; 1.54 A; A=1-260.
PDB; 3P3H; X-ray; 1.50 A; A=1-260.
PDB; 3P3J; X-ray; 1.60 A; A=1-260.
PDB; 3P44; X-ray; 2.20 A; A=1-260.
PDB; 3P4V; X-ray; 2.00 A; A=1-260.
PDB; 3P55; X-ray; 2.00 A; A=1-260.
PDB; 3P58; X-ray; 1.49 A; A=1-260.
PDB; 3P5A; X-ray; 1.49 A; A=1-260.
PDB; 3P5L; X-ray; 1.50 A; A=1-260.
PDB; 3PJJ; X-ray; 1.80 A; A=2-260.
PDB; 3PO6; X-ray; 1.47 A; A=2-260.
PDB; 3PYK; X-ray; 1.30 A; A=1-260.
PDB; 3QYK; X-ray; 1.47 A; A=1-260.
PDB; 3R16; X-ray; 1.60 A; A=4-260.
PDB; 3R17; X-ray; 1.70 A; B=4-260.
PDB; 3RG3; X-ray; 1.90 A; A=1-260.
PDB; 3RG4; X-ray; 1.50 A; A=1-260.
PDB; 3RGE; X-ray; 2.10 A; A=1-260.
PDB; 3RJ7; X-ray; 1.20 A; A=3-260.
PDB; 3RLD; X-ray; 1.50 A; A=1-260.
PDB; 3RYJ; X-ray; 1.39 A; B=2-260.
PDB; 3RYV; X-ray; 1.20 A; B=2-260.
PDB; 3RYX; X-ray; 1.60 A; B=2-260.
PDB; 3RYY; X-ray; 1.16 A; A=2-260.
PDB; 3RYZ; X-ray; 1.37 A; A=2-260.
PDB; 3RZ0; X-ray; 1.80 A; B=2-260.
PDB; 3RZ1; X-ray; 1.51 A; B=2-260.
PDB; 3RZ5; X-ray; 1.65 A; A=2-260.
PDB; 3RZ7; X-ray; 1.80 A; A=2-260.
PDB; 3RZ8; X-ray; 1.70 A; A=2-260.
PDB; 3S71; X-ray; 1.25 A; B=3-260.
PDB; 3S72; X-ray; 1.60 A; B=3-260.
PDB; 3S73; X-ray; 1.75 A; B=3-260.
PDB; 3S74; X-ray; 1.40 A; B=3-260.
PDB; 3S75; X-ray; 1.50 A; B=3-260.
PDB; 3S76; X-ray; 1.60 A; A=3-260.
PDB; 3S77; X-ray; 1.86 A; B=3-260.
PDB; 3S78; X-ray; 1.98 A; B=3-260.
PDB; 3S8X; X-ray; 1.30 A; A=1-260.
PDB; 3S9T; X-ray; 1.30 A; A=1-260.
PDB; 3SAP; X-ray; 1.75 A; A=1-260.
PDB; 3SAX; X-ray; 1.10 A; A=1-260.
PDB; 3SBH; X-ray; 1.65 A; A=1-260.
PDB; 3SBI; X-ray; 1.40 A; A=1-260.
PDB; 3T5U; X-ray; 1.75 A; A=2-260.
PDB; 3T5Z; X-ray; 1.65 A; A=2-260.
PDB; 3T82; X-ray; 2.00 A; A=1-260.
PDB; 3T83; X-ray; 1.80 A; A=1-260.
PDB; 3T84; X-ray; 2.00 A; A=1-260.
PDB; 3T85; X-ray; 2.40 A; A=1-260.
PDB; 3TMJ; Other; 2.00 A; A=3-260.
PDB; 3TVN; X-ray; 1.50 A; X=3-260.
PDB; 3TVO; X-ray; 1.60 A; X=3-260.
PDB; 3U3A; X-ray; 1.55 A; X=1-260.
PDB; 3U45; X-ray; 1.70 A; X=1-260.
PDB; 3U47; X-ray; 1.60 A; A=1-260.
PDB; 3U7C; X-ray; 0.93 A; A=1-260.
PDB; 3V2J; X-ray; 1.70 A; A=1-260.
PDB; 3V2M; X-ray; 1.47 A; A=1-260.
PDB; 3V3F; X-ray; 2.00 A; A=1-260.
PDB; 3V3G; X-ray; 1.56 A; B=1-260.
PDB; 3V3H; X-ray; 1.85 A; B=1-260.
PDB; 3V3I; X-ray; 1.73 A; B=1-260.
PDB; 3V3J; X-ray; 1.63 A; A=1-260.
PDB; 3V5G; X-ray; 1.50 A; A=1-260.
PDB; 3V7X; X-ray; 1.03 A; A=2-260.
PDB; 3VBD; X-ray; 1.05 A; A=2-260.
PDB; 3ZP9; X-ray; 1.31 A; A=1-260.
PDB; 4BCW; X-ray; 1.50 A; A=4-260.
PDB; 4BF1; X-ray; 1.35 A; A=2-260.
PDB; 4BF6; X-ray; 1.82 A; A=2-260.
PDB; 4CA2; X-ray; 2.10 A; A=1-260.
PDB; 4CAC; X-ray; 2.20 A; A=2-260.
PDB; 4CQ0; X-ray; 1.45 A; A=1-260.
PDB; 4DZ7; X-ray; 1.49 A; A=1-260.
PDB; 4DZ9; X-ray; 1.49 A; A=1-260.
PDB; 4E3D; X-ray; 1.60 A; A=1-260.
PDB; 4E3F; X-ray; 1.50 A; A=1-260.
PDB; 4E3G; X-ray; 1.55 A; A=1-260.
PDB; 4E3H; X-ray; 1.50 A; A=1-260.
PDB; 4E49; X-ray; 1.45 A; A=1-260.
PDB; 4E4A; X-ray; 1.45 A; A=1-260.
PDB; 4E5Q; X-ray; 1.70 A; A=1-260.
PDB; 4FIK; X-ray; 1.20 A; A=1-260.
PDB; 4FL7; X-ray; 1.85 A; A=2-260.
PDB; 4FPT; X-ray; 0.98 A; A=1-260.
PDB; 4FRC; X-ray; 0.98 A; A=1-260.
PDB; 4FU5; X-ray; 0.98 A; A=1-260.
PDB; 4FVN; X-ray; 1.05 A; A=1-260.
PDB; 4FVO; X-ray; 1.05 A; A=1-260.
PDB; 4G0C; Neutron; 2.00 A; A=4-260.
PDB; 4GL1; X-ray; 1.50 A; X=1-260.
PDB; 4HBA; X-ray; 1.76 A; A=1-260.
PDB; 4HEW; X-ray; 1.70 A; A=1-260.
PDB; 4HEY; X-ray; 1.45 A; A=1-260.
PDB; 4HEZ; X-ray; 1.34 A; A=1-260.
PDB; 4HF3; X-ray; 1.15 A; A=1-260.
PDB; 4HT0; X-ray; 1.60 A; A=1-260.
PDB; 4IDR; X-ray; 1.60 A; X=3-260.
PDB; 4ILX; X-ray; 1.60 A; A=4-260.
PDB; 4ITO; X-ray; 1.16 A; A=1-260.
PDB; 4ITP; X-ray; 1.70 A; A=4-260.
PDB; 4IWZ; X-ray; 1.60 A; A=4-260.
PDB; 4JS6; X-ray; 1.55 A; A=1-260.
PDB; 4JSA; X-ray; 1.50 A; A=1-260.
PDB; 4JSS; X-ray; 1.50 A; A=1-260.
PDB; 4JSW; X-ray; 1.90 A; A=1-260.
PDB; 4JSZ; X-ray; 1.90 A; A=1-260.
PDB; 4K0S; X-ray; 1.80 A; A=4-260.
PDB; 4K0T; X-ray; 1.78 A; A=4-260.
PDB; 4K0Z; X-ray; 1.80 A; A=3-260.
PDB; 4K13; X-ray; 1.60 A; A=4-260.
PDB; 4K1Q; X-ray; 1.70 A; A=3-260.
PDB; 4KAP; X-ray; 1.45 A; A=5-260.
PDB; 4KNI; X-ray; 1.80 A; A=1-260.
PDB; 4KNJ; X-ray; 2.00 A; A=1-260.
PDB; 4KUV; X-ray; 1.35 A; A=5-260.
PDB; 4KUW; X-ray; 1.55 A; A=4-260.
PDB; 4KUY; X-ray; 1.65 A; A=4-260.
PDB; 4KV0; X-ray; 1.55 A; A=4-260.
PDB; 4L5U; X-ray; 2.05 A; A=1-260.
PDB; 4L5V; X-ray; 1.63 A; A=1-260.
PDB; 4L5W; X-ray; 1.70 A; A=1-260.
PDB; 4LHI; X-ray; 1.60 A; A=1-260.
PDB; 4LP6; X-ray; 2.15 A; A/B=1-260.
PDB; 4M2R; X-ray; 1.99 A; A=4-260.
PDB; 4M2U; X-ray; 2.00 A; A=4-260.
PDB; 4M2V; X-ray; 1.72 A; A=4-260.
PDB; 4M2W; X-ray; 1.66 A; A=4-260.
PDB; 4MDG; X-ray; 1.35 A; A=3-260.
PDB; 4MDL; X-ray; 1.52 A; A=3-260.
PDB; 4MDM; X-ray; 1.55 A; A=3-260.
PDB; 4MLT; X-ray; 2.00 A; A=1-260.
PDB; 4MLX; X-ray; 1.65 A; A=1-260.
PDB; 4MO8; X-ray; 1.85 A; A=1-260.
PDB; 4MTY; X-ray; 1.00 A; A=1-260.
PDB; 4N0X; X-ray; 1.63 A; B=1-260.
PDB; 4N16; X-ray; 1.54 A; A=1-260.
PDB; 4PQ7; X-ray; 1.85 A; A=1-260.
PDB; 4PXX; X-ray; 1.85 A; A=1-260.
PDB; 4PYX; X-ray; 1.80 A; A=1-260.
PDB; 4PYY; X-ray; 1.75 A; A=1-260.
PDB; 4PZH; X-ray; 1.06 A; A=1-260.
PDB; 4Q06; X-ray; 1.15 A; A=1-260.
PDB; 4Q07; X-ray; 1.15 A; A=1-260.
PDB; 4Q08; X-ray; 1.07 A; A=1-260.
PDB; 4Q09; X-ray; 1.20 A; A=1-260.
PDB; 4Q49; Neutron; 1.80 A; A=1-260.
PDB; 4Q6D; X-ray; 1.12 A; A=1-260.
PDB; 4Q6E; X-ray; 1.12 A; A=1-260.
PDB; 4Q78; X-ray; 1.00 A; A=3-260.
PDB; 4Q7P; X-ray; 1.65 A; A=1-260.
PDB; 4Q7S; X-ray; 1.80 A; A=1-260.
PDB; 4Q7V; X-ray; 1.60 A; A=1-260.
PDB; 4Q7W; X-ray; 1.45 A; A=1-260.
PDB; 4Q81; X-ray; 1.55 A; A=1-260.
PDB; 4Q83; X-ray; 1.55 A; A=1-260.
PDB; 4Q87; X-ray; 1.55 A; A=1-260.
PDB; 4Q8X; X-ray; 1.55 A; A=1-260.
PDB; 4Q8Y; X-ray; 1.45 A; A=1-260.
PDB; 4Q8Z; X-ray; 1.50 A; A=1-260.
PDB; 4Q90; X-ray; 1.54 A; A=1-260.
PDB; 4Q99; X-ray; 1.50 A; A=1-260.
PDB; 4Q9Y; X-ray; 1.55 A; A=1-260.
PDB; 4QEF; X-ray; 1.47 A; A=1-260.
PDB; 4QIY; X-ray; 1.30 A; A/B/C/D=1-260.
PDB; 4QJM; X-ray; 1.75 A; A=1-260.
PDB; 4QK1; X-ray; 1.60 A; A=1-260.
PDB; 4QK2; X-ray; 1.52 A; A=1-260.
PDB; 4QK3; X-ray; 1.34 A; A=1-260.
PDB; 4QSA; X-ray; 1.50 A; A=1-260.
PDB; 4QSB; X-ray; 1.40 A; A=1-260.
PDB; 4QSI; X-ray; 1.95 A; A=1-260.
PDB; 4QTL; X-ray; 1.80 A; A=1-260.
PDB; 4QY3; X-ray; 1.50 A; A=2-260.
PDB; 4R59; X-ray; 1.65 A; A=1-260.
PDB; 4R5A; X-ray; 1.64 A; A=1-260.
PDB; 4R5B; X-ray; 1.50 A; A=1-260.
PDB; 4RFC; X-ray; 1.65 A; A=1-260.
PDB; 4RFD; X-ray; 1.63 A; A=1-260.
PDB; 4RH2; X-ray; 1.30 A; A=1-260.
PDB; 4RIU; X-ray; 1.65 A; A=1-260.
PDB; 4RIV; X-ray; 1.63 A; A=1-260.
PDB; 4RN4; X-ray; 1.53 A; A=1-260.
PDB; 4RUX; X-ray; 1.14 A; A=1-260.
PDB; 4RUY; X-ray; 1.14 A; A=1-260.
PDB; 4RUZ; X-ray; 1.63 A; A=1-260.
PDB; 4WL4; X-ray; 1.10 A; A=1-260.
PDB; 4WW6; X-ray; 1.06 A; A=1-260.
PDB; 4XE1; X-ray; 1.80 A; A=1-260.
PDB; 4Y0J; Neutron; 2.00 A; A=3-260.
PDB; 4YGJ; X-ray; 1.10 A; A=3-260.
PDB; 4YGK; X-ray; 1.50 A; A=3-260.
PDB; 4YGL; X-ray; 1.51 A; A=3-260.
PDB; 4YGN; X-ray; 1.23 A; A=3-260.
PDB; 4YVY; X-ray; 1.45 A; A=2-260.
PDB; 4YWP; X-ray; 1.45 A; A=4-260.
PDB; 4YX4; X-ray; 1.01 A; A=1-260.
PDB; 4YXI; X-ray; 0.96 A; A=1-260.
PDB; 4YXO; X-ray; 1.06 A; A=1-260.
PDB; 4YXU; X-ray; 1.08 A; A=1-260.
PDB; 4YYT; X-ray; 1.07 A; A=1-260.
PDB; 4Z0Q; X-ray; 1.45 A; A=3-260.
PDB; 4Z1E; X-ray; 2.01 A; A=2-260.
PDB; 4Z1J; X-ray; 1.27 A; A=3-260.
PDB; 4Z1K; X-ray; 1.35 A; A=4-260.
PDB; 4Z1N; X-ray; 1.47 A; A=3-260.
PDB; 4ZAO; X-ray; 1.80 A; A=1-257.
PDB; 4ZWI; X-ray; 1.60 A; A=4-260.
PDB; 4ZWX; X-ray; 1.70 A; A=4-260.
PDB; 4ZWY; X-ray; 1.50 A; A=4-260.
PDB; 4ZWZ; X-ray; 1.62 A; A=4-260.
PDB; 4ZX0; X-ray; 1.60 A; A=4-260.
PDB; 4ZX1; X-ray; 1.50 A; A=4-260.
PDB; 5A6H; X-ray; 1.57 A; A=1-260.
PDB; 5AMD; X-ray; 1.50 A; A=2-260.
PDB; 5AMG; X-ray; 1.55 A; A=2-260.
PDB; 5AML; X-ray; 1.36 A; A=2-260.
PDB; 5BNL; X-ray; 2.00 A; A=4-260.
PDB; 5BRU; X-ray; 1.60 A; A=3-260.
PDB; 5BRV; X-ray; 1.60 A; A=3-260.
PDB; 5BRW; X-ray; 1.40 A; A=1-260.
PDB; 5BYI; X-ray; 1.15 A; A=1-260.
PDB; 5C8I; Other; 1.56 A; A=1-260.
PDB; 5CA2; X-ray; 2.10 A; A=1-260.
PDB; 5CAC; X-ray; 2.20 A; A=2-260.
PDB; 5CJL; X-ray; 1.20 A; A=4-260.
PDB; 5CLU; X-ray; 1.55 A; A=4-260.
PDB; 5DOG; X-ray; 1.70 A; A=1-260.
PDB; 5DOH; X-ray; 1.05 A; A/B=1-260.
PDB; 5DRS; X-ray; 1.10 A; A=1-260.
PDB; 5DSI; X-ray; 1.20 A; A=1-260.
PDB; 5DSJ; X-ray; 1.25 A; A=1-260.
PDB; 5DSK; X-ray; 1.30 A; A=1-260.
PDB; 5DSL; X-ray; 1.45 A; A=1-260.
PDB; 5DSM; X-ray; 1.30 A; A=1-260.
PDB; 5DSN; X-ray; 1.45 A; A=1-260.
PDB; 5DSO; X-ray; 1.40 A; A=1-260.
PDB; 5DSP; X-ray; 1.40 A; A=1-260.
PDB; 5DSQ; X-ray; 1.50 A; A=1-260.
PDB; 5DSR; X-ray; 1.30 A; A=1-260.
PDB; 5E28; X-ray; 1.30 A; A=4-260.
PDB; 5E2K; X-ray; 1.40 A; A=4-260.
PDB; 5E2R; X-ray; 1.60 A; A=1-260.
PDB; 5E2S; X-ray; 1.50 A; A=3-260.
PDB; 5EH5; X-ray; 1.21 A; A=1-260.
PDB; 5EH7; X-ray; 1.43 A; A=1-260.
PDB; 5EH8; X-ray; 1.38 A; A=1-260.
PDB; 5EHE; X-ray; 1.50 A; A=1-260.
PDB; 5EHV; X-ray; 1.21 A; A=1-260.
PDB; 5EHW; X-ray; 1.39 A; A=1-260.
PDB; 5EIJ; X-ray; 1.99 A; A=4-260.
PDB; 5EKH; X-ray; 1.34 A; A=1-260.
PDB; 5EKJ; X-ray; 1.13 A; A=1-260.
PDB; 5EKM; X-ray; 1.33 A; A=1-260.
PDB; 5EOI; X-ray; 1.80 A; A=3-260.
PDB; 5FDC; X-ray; 1.75 A; A=1-260.
PDB; 5FDI; X-ray; 1.85 A; A=1-260.
PDB; 5FLO; X-ray; 1.66 A; A=1-260.
PDB; 5FLP; X-ray; 1.71 A; A=1-260.
PDB; 5FLQ; X-ray; 1.70 A; A=1-260.
PDB; 5FLR; X-ray; 1.68 A; A=1-260.
PDB; 5FLS; X-ray; 1.67 A; A=1-260.
PDB; 5FLT; X-ray; 1.67 A; A=1-260.
PDB; 5FNG; X-ray; 2.05 A; A=1-260.
PDB; 5FNH; X-ray; 1.66 A; A=1-260.
PDB; 5FNI; X-ray; 1.60 A; A=1-260.
PDB; 5FNJ; X-ray; 1.67 A; A=1-260.
PDB; 5FNK; X-ray; 1.59 A; A=1-260.
PDB; 5FNL; X-ray; 1.59 A; A=1-260.
PDB; 5FNM; X-ray; 1.59 A; A=1-260.
PDB; 5G01; X-ray; 1.40 A; A=1-260.
PDB; 5G03; X-ray; 1.35 A; A=1-260.
PDB; 5G0B; X-ray; 1.55 A; A=1-260.
PDB; 5G0C; X-ray; 1.28 A; A=1-260.
PDB; 5GMN; X-ray; 1.80 A; A=1-260.
PDB; 5J8Z; X-ray; 1.70 A; A=1-260.
PDB; 5JDV; X-ray; 1.34 A; B=3-260.
PDB; 5JE7; X-ray; 1.15 A; B=4-260.
PDB; 5JEG; X-ray; 1.19 A; B=3-260.
PDB; 5JEH; X-ray; 1.13 A; B=3-260.
PDB; 5JEP; X-ray; 1.19 A; B=3-260.
PDB; 5JES; X-ray; 1.21 A; B=3-259.
PDB; 5JG3; X-ray; 1.21 A; B=3-260.
PDB; 5JG5; X-ray; 1.19 A; B=3-260.
PDB; 5JGS; X-ray; 1.11 A; B=4-260.
PDB; 5JGT; X-ray; 1.10 A; B=3-260.
PDB; 5JMZ; X-ray; 1.90 A; A=4-260.
PDB; 5JN1; X-ray; 1.52 A; A=4-260.
PDB; 5JN3; X-ray; 1.60 A; A=4-260.
PDB; 5JN7; X-ray; 1.52 A; A=4-260.
PDB; 5JQ0; X-ray; 1.40 A; A=1-260.
PDB; 5JQT; X-ray; 1.36 A; A=1-260.
PDB; 5L3O; X-ray; 1.98 A; A/B=1-260.
PDB; 5L6K; X-ray; 1.70 A; A/B=1-260.
PDB; 5L6T; X-ray; 2.65 A; A/B=1-260.
PDB; 5L70; X-ray; 2.20 A; A/B=1-260.
PDB; 5L9E; X-ray; 2.90 A; A/B/C/D=1-260.
PDB; 5LJQ; X-ray; 1.05 A; A=3-260.
PDB; 5LJT; X-ray; 1.00 A; A=3-260.
PDB; 5LL4; X-ray; 1.12 A; A/B=1-260.
PDB; 5LL8; X-ray; 1.03 A; A=1-260.
PDB; 5LLC; X-ray; 1.10 A; A=1-260.
PDB; 5LLE; X-ray; 1.90 A; A=1-260.
PDB; 5LLG; X-ray; 1.12 A; A=1-260.
PDB; 5LLH; X-ray; 1.90 A; A=1-260.
PDB; 5LMD; X-ray; 1.70 A; A=1-260.
PDB; 5LVS; X-ray; 1.42 A; A/B=2-260.
PDB; 5N0D; X-ray; 1.70 A; A=1-260.
PDB; 5N0E; X-ray; 1.75 A; A=1-260.
PDB; 5O07; X-ray; 1.80 A; A=1-260.
PDB; 5SZ0; X-ray; 1.63 A; A=4-260.
PDB; 5SZ1; X-ray; 1.55 A; A=4-260.
PDB; 5SZ2; X-ray; 1.63 A; A=4-260.
PDB; 5SZ3; X-ray; 1.69 A; A=4-260.
PDB; 5SZ4; X-ray; 1.60 A; A=4-260.
PDB; 5SZ5; X-ray; 1.27 A; A=4-260.
PDB; 5SZ6; X-ray; 1.15 A; A=4-260.
PDB; 5SZ7; X-ray; 1.78 A; A=4-260.
PDB; 5T71; X-ray; 1.30 A; A=1-260.
PDB; 5T72; X-ray; 1.30 A; A=1-260.
PDB; 5T74; X-ray; 1.20 A; A=1-260.
PDB; 5T75; X-ray; 1.50 A; A=1-260.
PDB; 5TFX; X-ray; 1.50 A; A=1-260.
PDB; 5TH4; X-ray; 1.47 A; A=1-260.
PDB; 5THI; X-ray; 1.50 A; A=1-260.
PDB; 5THJ; X-ray; 1.50 A; A=1-260.
PDB; 5THN; X-ray; 1.33 A; A=1-260.
PDB; 5TI0; X-ray; 1.42 A; A=1-260.
PDB; 5TXY; X-ray; 1.21 A; A=1-260.
PDB; 5TY1; X-ray; 1.60 A; A=1-260.
PDB; 5TY8; X-ray; 1.45 A; A=1-260.
PDB; 5TY9; X-ray; 1.53 A; A=1-260.
PDB; 5TYA; X-ray; 1.50 A; A=1-260.
PDB; 5U0D; X-ray; 1.59 A; A=1-260.
PDB; 5U0E; X-ray; 1.27 A; A=1-260.
PDB; 5U0F; X-ray; 1.21 A; A=1-260.
PDB; 5U0G; X-ray; 1.54 A; A=1-260.
PDB; 5ULN; X-ray; 1.35 A; A=1-260.
PDB; 5VGY; X-ray; 1.39 A; A=1-260.
PDB; 5WEX; X-ray; 1.26 A; A=1-260.
PDB; 6CA2; X-ray; 2.50 A; A=1-260.
PDB; 7CA2; X-ray; 2.40 A; A=1-260.
PDB; 8CA2; X-ray; 2.40 A; A=1-260.
PDB; 9CA2; X-ray; 2.80 A; A=1-260.
PDBsum; 12CA; -.
PDBsum; 1A42; -.
PDBsum; 1AM6; -.
PDBsum; 1AVN; -.
PDBsum; 1BCD; -.
PDBsum; 1BIC; -.
PDBsum; 1BN1; -.
PDBsum; 1BN3; -.
PDBsum; 1BN4; -.
PDBsum; 1BNM; -.
PDBsum; 1BNN; -.
PDBsum; 1BNQ; -.
PDBsum; 1BNT; -.
PDBsum; 1BNU; -.
PDBsum; 1BNV; -.
PDBsum; 1BNW; -.
PDBsum; 1BV3; -.
PDBsum; 1CA2; -.
PDBsum; 1CA3; -.
PDBsum; 1CAH; -.
PDBsum; 1CAI; -.
PDBsum; 1CAJ; -.
PDBsum; 1CAK; -.
PDBsum; 1CAL; -.
PDBsum; 1CAM; -.
PDBsum; 1CAN; -.
PDBsum; 1CAO; -.
PDBsum; 1CAY; -.
PDBsum; 1CAZ; -.
PDBsum; 1CCS; -.
PDBsum; 1CCT; -.
PDBsum; 1CCU; -.
PDBsum; 1CIL; -.
PDBsum; 1CIM; -.
PDBsum; 1CIN; -.
PDBsum; 1CNB; -.
PDBsum; 1CNC; -.
PDBsum; 1CNG; -.
PDBsum; 1CNH; -.
PDBsum; 1CNI; -.
PDBsum; 1CNJ; -.
PDBsum; 1CNK; -.
PDBsum; 1CNW; -.
PDBsum; 1CNX; -.
PDBsum; 1CNY; -.
PDBsum; 1CRA; -.
PDBsum; 1CVA; -.
PDBsum; 1CVB; -.
PDBsum; 1CVC; -.
PDBsum; 1CVD; -.
PDBsum; 1CVE; -.
PDBsum; 1CVF; -.
PDBsum; 1CVH; -.
PDBsum; 1DCA; -.
PDBsum; 1DCB; -.
PDBsum; 1EOU; -.
PDBsum; 1F2W; -.
PDBsum; 1FQL; -.
PDBsum; 1FQM; -.
PDBsum; 1FQN; -.
PDBsum; 1FQR; -.
PDBsum; 1FR4; -.
PDBsum; 1FR7; -.
PDBsum; 1FSN; -.
PDBsum; 1FSQ; -.
PDBsum; 1FSR; -.
PDBsum; 1G0E; -.
PDBsum; 1G0F; -.
PDBsum; 1G1D; -.
PDBsum; 1G3Z; -.
PDBsum; 1G45; -.
PDBsum; 1G46; -.
PDBsum; 1G48; -.
PDBsum; 1G4J; -.
PDBsum; 1G4O; -.
PDBsum; 1G52; -.
PDBsum; 1G53; -.
PDBsum; 1G54; -.
PDBsum; 1H4N; -.
PDBsum; 1H9N; -.
PDBsum; 1H9Q; -.
PDBsum; 1HCA; -.
PDBsum; 1HEA; -.
PDBsum; 1HEB; -.
PDBsum; 1HEC; -.
PDBsum; 1HED; -.
PDBsum; 1HVA; -.
PDBsum; 1I8Z; -.
PDBsum; 1I90; -.
PDBsum; 1I91; -.
PDBsum; 1I9L; -.
PDBsum; 1I9M; -.
PDBsum; 1I9N; -.
PDBsum; 1I9O; -.
PDBsum; 1I9P; -.
PDBsum; 1I9Q; -.
PDBsum; 1IF4; -.
PDBsum; 1IF5; -.
PDBsum; 1IF6; -.
PDBsum; 1IF7; -.
PDBsum; 1IF8; -.
PDBsum; 1IF9; -.
PDBsum; 1KWQ; -.
PDBsum; 1KWR; -.
PDBsum; 1LG5; -.
PDBsum; 1LG6; -.
PDBsum; 1LGD; -.
PDBsum; 1LUG; -.
PDBsum; 1LZV; -.
PDBsum; 1MOO; -.
PDBsum; 1MUA; -.
PDBsum; 1OKL; -.
PDBsum; 1OKM; -.
PDBsum; 1OKN; -.
PDBsum; 1OQ5; -.
PDBsum; 1RAY; -.
PDBsum; 1RAZ; -.
PDBsum; 1RZA; -.
PDBsum; 1RZB; -.
PDBsum; 1RZC; -.
PDBsum; 1RZD; -.
PDBsum; 1RZE; -.
PDBsum; 1T9N; -.
PDBsum; 1TB0; -.
PDBsum; 1TBT; -.
PDBsum; 1TE3; -.
PDBsum; 1TEQ; -.
PDBsum; 1TEU; -.
PDBsum; 1TG3; -.
PDBsum; 1TG9; -.
PDBsum; 1TH9; -.
PDBsum; 1THK; -.
PDBsum; 1TTM; -.
PDBsum; 1UGA; -.
PDBsum; 1UGB; -.
PDBsum; 1UGC; -.
PDBsum; 1UGD; -.
PDBsum; 1UGE; -.
PDBsum; 1UGF; -.
PDBsum; 1UGG; -.
PDBsum; 1XEG; -.
PDBsum; 1XEV; -.
PDBsum; 1XPZ; -.
PDBsum; 1XQ0; -.
PDBsum; 1YDA; -.
PDBsum; 1YDB; -.
PDBsum; 1YDC; -.
PDBsum; 1YDD; -.
PDBsum; 1YO0; -.
PDBsum; 1YO1; -.
PDBsum; 1YO2; -.
PDBsum; 1Z9Y; -.
PDBsum; 1ZE8; -.
PDBsum; 1ZFK; -.
PDBsum; 1ZFQ; -.
PDBsum; 1ZGE; -.
PDBsum; 1ZGF; -.
PDBsum; 1ZH9; -.
PDBsum; 1ZSA; -.
PDBsum; 1ZSB; -.
PDBsum; 1ZSC; -.
PDBsum; 2ABE; -.
PDBsum; 2AW1; -.
PDBsum; 2AX2; -.
PDBsum; 2CA2; -.
PDBsum; 2CBA; -.
PDBsum; 2CBB; -.
PDBsum; 2CBC; -.
PDBsum; 2CBD; -.
PDBsum; 2CBE; -.
PDBsum; 2EU2; -.
PDBsum; 2EU3; -.
PDBsum; 2EZ7; -.
PDBsum; 2F14; -.
PDBsum; 2FMG; -.
PDBsum; 2FMZ; -.
PDBsum; 2FNK; -.
PDBsum; 2FNM; -.
PDBsum; 2FNN; -.
PDBsum; 2FOQ; -.
PDBsum; 2FOS; -.
PDBsum; 2FOU; -.
PDBsum; 2FOV; -.
PDBsum; 2GD8; -.
PDBsum; 2GEH; -.
PDBsum; 2H15; -.
PDBsum; 2H4N; -.
PDBsum; 2HD6; -.
PDBsum; 2HKK; -.
PDBsum; 2HL4; -.
PDBsum; 2HNC; -.
PDBsum; 2HOC; -.
PDBsum; 2ILI; -.
PDBsum; 2NNG; -.
PDBsum; 2NNO; -.
PDBsum; 2NNS; -.
PDBsum; 2NNV; -.
PDBsum; 2NWO; -.
PDBsum; 2NWP; -.
PDBsum; 2NWY; -.
PDBsum; 2NWZ; -.
PDBsum; 2NXR; -.
PDBsum; 2NXS; -.
PDBsum; 2NXT; -.
PDBsum; 2O4Z; -.
PDBsum; 2OSF; -.
PDBsum; 2OSM; -.
PDBsum; 2POU; -.
PDBsum; 2POV; -.
PDBsum; 2POW; -.
PDBsum; 2Q1B; -.
PDBsum; 2Q1Q; -.
PDBsum; 2Q38; -.
PDBsum; 2QO8; -.
PDBsum; 2QOA; -.
PDBsum; 2QP6; -.
PDBsum; 2VVA; -.
PDBsum; 2VVB; -.
PDBsum; 2WD2; -.
PDBsum; 2WD3; -.
PDBsum; 2WEG; -.
PDBsum; 2WEH; -.
PDBsum; 2WEJ; -.
PDBsum; 2WEO; -.
PDBsum; 2X7S; -.
PDBsum; 2X7T; -.
PDBsum; 2X7U; -.
PDBsum; 3B4F; -.
PDBsum; 3BET; -.
PDBsum; 3BL0; -.
PDBsum; 3BL1; -.
PDBsum; 3C7P; -.
PDBsum; 3CA2; -.
PDBsum; 3CAJ; -.
PDBsum; 3CYU; -.
PDBsum; 3D8W; -.
PDBsum; 3D92; -.
PDBsum; 3D93; -.
PDBsum; 3D9Z; -.
PDBsum; 3DAZ; -.
PDBsum; 3DBU; -.
PDBsum; 3DC3; -.
PDBsum; 3DC9; -.
PDBsum; 3DCC; -.
PDBsum; 3DCS; -.
PDBsum; 3DCW; -.
PDBsum; 3DD0; -.
PDBsum; 3DD8; -.
PDBsum; 3DV7; -.
PDBsum; 3DVB; -.
PDBsum; 3DVC; -.
PDBsum; 3DVD; -.
PDBsum; 3EFI; -.
PDBsum; 3EFT; -.
PDBsum; 3F4X; -.
PDBsum; 3F8E; -.
PDBsum; 3FFP; -.
PDBsum; 3GZ0; -.
PDBsum; 3HFP; -.
PDBsum; 3HKN; -.
PDBsum; 3HKQ; -.
PDBsum; 3HKT; -.
PDBsum; 3HKU; -.
PDBsum; 3HLJ; -.
PDBsum; 3HS4; -.
PDBsum; 3IBI; -.
PDBsum; 3IBL; -.
PDBsum; 3IBN; -.
PDBsum; 3IBU; -.
PDBsum; 3IEO; -.
PDBsum; 3IGP; -.
PDBsum; 3K2F; -.
PDBsum; 3K34; -.
PDBsum; 3K7K; -.
PDBsum; 3KIG; -.
PDBsum; 3KKX; -.
PDBsum; 3KNE; -.
PDBsum; 3KOI; -.
PDBsum; 3KOK; -.
PDBsum; 3KON; -.
PDBsum; 3KS3; -.
PDBsum; 3KWA; -.
PDBsum; 3L14; -.
PDBsum; 3M04; -.
PDBsum; 3M14; -.
PDBsum; 3M1J; -.
PDBsum; 3M1K; -.
PDBsum; 3M1Q; -.
PDBsum; 3M1W; -.
PDBsum; 3M2N; -.
PDBsum; 3M2X; -.
PDBsum; 3M2Y; -.
PDBsum; 3M2Z; -.
PDBsum; 3M3X; -.
PDBsum; 3M40; -.
PDBsum; 3M5E; -.
PDBsum; 3M5S; -.
PDBsum; 3M5T; -.
PDBsum; 3M67; -.
PDBsum; 3M96; -.
PDBsum; 3M98; -.
PDBsum; 3MHC; -.
PDBsum; 3MHI; -.
PDBsum; 3MHL; -.
PDBsum; 3MHM; -.
PDBsum; 3MHO; -.
PDBsum; 3ML2; -.
PDBsum; 3MMF; -.
PDBsum; 3MNA; -.
PDBsum; 3MNH; -.
PDBsum; 3MNI; -.
PDBsum; 3MNJ; -.
PDBsum; 3MNK; -.
PDBsum; 3MNU; -.
PDBsum; 3MWO; -.
PDBsum; 3MYQ; -.
PDBsum; 3MZC; -.
PDBsum; 3N0N; -.
PDBsum; 3N2P; -.
PDBsum; 3N3J; -.
PDBsum; 3N4B; -.
PDBsum; 3NB5; -.
PDBsum; 3NI5; -.
PDBsum; 3NJ9; -.
PDBsum; 3OIK; -.
PDBsum; 3OIL; -.
PDBsum; 3OIM; -.
PDBsum; 3OKU; -.
PDBsum; 3OKV; -.
PDBsum; 3OY0; -.
PDBsum; 3OYQ; -.
PDBsum; 3OYS; -.
PDBsum; 3P3H; -.
PDBsum; 3P3J; -.
PDBsum; 3P44; -.
PDBsum; 3P4V; -.
PDBsum; 3P55; -.
PDBsum; 3P58; -.
PDBsum; 3P5A; -.
PDBsum; 3P5L; -.
PDBsum; 3PJJ; -.
PDBsum; 3PO6; -.
PDBsum; 3PYK; -.
PDBsum; 3QYK; -.
PDBsum; 3R16; -.
PDBsum; 3R17; -.
PDBsum; 3RG3; -.
PDBsum; 3RG4; -.
PDBsum; 3RGE; -.
PDBsum; 3RJ7; -.
PDBsum; 3RLD; -.
PDBsum; 3RYJ; -.
PDBsum; 3RYV; -.
PDBsum; 3RYX; -.
PDBsum; 3RYY; -.
PDBsum; 3RYZ; -.
PDBsum; 3RZ0; -.
PDBsum; 3RZ1; -.
PDBsum; 3RZ5; -.
PDBsum; 3RZ7; -.
PDBsum; 3RZ8; -.
PDBsum; 3S71; -.
PDBsum; 3S72; -.
PDBsum; 3S73; -.
PDBsum; 3S74; -.
PDBsum; 3S75; -.
PDBsum; 3S76; -.
PDBsum; 3S77; -.
PDBsum; 3S78; -.
PDBsum; 3S8X; -.
PDBsum; 3S9T; -.
PDBsum; 3SAP; -.
PDBsum; 3SAX; -.
PDBsum; 3SBH; -.
PDBsum; 3SBI; -.
PDBsum; 3T5U; -.
PDBsum; 3T5Z; -.
PDBsum; 3T82; -.
PDBsum; 3T83; -.
PDBsum; 3T84; -.
PDBsum; 3T85; -.
PDBsum; 3TMJ; -.
PDBsum; 3TVN; -.
PDBsum; 3TVO; -.
PDBsum; 3U3A; -.
PDBsum; 3U45; -.
PDBsum; 3U47; -.
PDBsum; 3U7C; -.
PDBsum; 3V2J; -.
PDBsum; 3V2M; -.
PDBsum; 3V3F; -.
PDBsum; 3V3G; -.
PDBsum; 3V3H; -.
PDBsum; 3V3I; -.
PDBsum; 3V3J; -.
PDBsum; 3V5G; -.
PDBsum; 3V7X; -.
PDBsum; 3VBD; -.
PDBsum; 3ZP9; -.
PDBsum; 4BCW; -.
PDBsum; 4BF1; -.
PDBsum; 4BF6; -.
PDBsum; 4CA2; -.
PDBsum; 4CAC; -.
PDBsum; 4CQ0; -.
PDBsum; 4DZ7; -.
PDBsum; 4DZ9; -.
PDBsum; 4E3D; -.
PDBsum; 4E3F; -.
PDBsum; 4E3G; -.
PDBsum; 4E3H; -.
PDBsum; 4E49; -.
PDBsum; 4E4A; -.
PDBsum; 4E5Q; -.
PDBsum; 4FIK; -.
PDBsum; 4FL7; -.
PDBsum; 4FPT; -.
PDBsum; 4FRC; -.
PDBsum; 4FU5; -.
PDBsum; 4FVN; -.
PDBsum; 4FVO; -.
PDBsum; 4G0C; -.
PDBsum; 4GL1; -.
PDBsum; 4HBA; -.
PDBsum; 4HEW; -.
PDBsum; 4HEY; -.
PDBsum; 4HEZ; -.
PDBsum; 4HF3; -.
PDBsum; 4HT0; -.
PDBsum; 4IDR; -.
PDBsum; 4ILX; -.
PDBsum; 4ITO; -.
PDBsum; 4ITP; -.
PDBsum; 4IWZ; -.
PDBsum; 4JS6; -.
PDBsum; 4JSA; -.
PDBsum; 4JSS; -.
PDBsum; 4JSW; -.
PDBsum; 4JSZ; -.
PDBsum; 4K0S; -.
PDBsum; 4K0T; -.
PDBsum; 4K0Z; -.
PDBsum; 4K13; -.
PDBsum; 4K1Q; -.
PDBsum; 4KAP; -.
PDBsum; 4KNI; -.
PDBsum; 4KNJ; -.
PDBsum; 4KUV; -.
PDBsum; 4KUW; -.
PDBsum; 4KUY; -.
PDBsum; 4KV0; -.
PDBsum; 4L5U; -.
PDBsum; 4L5V; -.
PDBsum; 4L5W; -.
PDBsum; 4LHI; -.
PDBsum; 4LP6; -.
PDBsum; 4M2R; -.
PDBsum; 4M2U; -.
PDBsum; 4M2V; -.
PDBsum; 4M2W; -.
PDBsum; 4MDG; -.
PDBsum; 4MDL; -.
PDBsum; 4MDM; -.
PDBsum; 4MLT; -.
PDBsum; 4MLX; -.
PDBsum; 4MO8; -.
PDBsum; 4MTY; -.
PDBsum; 4N0X; -.
PDBsum; 4N16; -.
PDBsum; 4PQ7; -.
PDBsum; 4PXX; -.
PDBsum; 4PYX; -.
PDBsum; 4PYY; -.
PDBsum; 4PZH; -.
PDBsum; 4Q06; -.
PDBsum; 4Q07; -.
PDBsum; 4Q08; -.
PDBsum; 4Q09; -.
PDBsum; 4Q49; -.
PDBsum; 4Q6D; -.
PDBsum; 4Q6E; -.
PDBsum; 4Q78; -.
PDBsum; 4Q7P; -.
PDBsum; 4Q7S; -.
PDBsum; 4Q7V; -.
PDBsum; 4Q7W; -.
PDBsum; 4Q81; -.
PDBsum; 4Q83; -.
PDBsum; 4Q87; -.
PDBsum; 4Q8X; -.
PDBsum; 4Q8Y; -.
PDBsum; 4Q8Z; -.
PDBsum; 4Q90; -.
PDBsum; 4Q99; -.
PDBsum; 4Q9Y; -.
PDBsum; 4QEF; -.
PDBsum; 4QIY; -.
PDBsum; 4QJM; -.
PDBsum; 4QK1; -.
PDBsum; 4QK2; -.
PDBsum; 4QK3; -.
PDBsum; 4QSA; -.
PDBsum; 4QSB; -.
PDBsum; 4QSI; -.
PDBsum; 4QTL; -.
PDBsum; 4QY3; -.
PDBsum; 4R59; -.
PDBsum; 4R5A; -.
PDBsum; 4R5B; -.
PDBsum; 4RFC; -.
PDBsum; 4RFD; -.
PDBsum; 4RH2; -.
PDBsum; 4RIU; -.
PDBsum; 4RIV; -.
PDBsum; 4RN4; -.
PDBsum; 4RUX; -.
PDBsum; 4RUY; -.
PDBsum; 4RUZ; -.
PDBsum; 4WL4; -.
PDBsum; 4WW6; -.
PDBsum; 4XE1; -.
PDBsum; 4Y0J; -.
PDBsum; 4YGJ; -.
PDBsum; 4YGK; -.
PDBsum; 4YGL; -.
PDBsum; 4YGN; -.
PDBsum; 4YVY; -.
PDBsum; 4YWP; -.
PDBsum; 4YX4; -.
PDBsum; 4YXI; -.
PDBsum; 4YXO; -.
PDBsum; 4YXU; -.
PDBsum; 4YYT; -.
PDBsum; 4Z0Q; -.
PDBsum; 4Z1E; -.
PDBsum; 4Z1J; -.
PDBsum; 4Z1K; -.
PDBsum; 4Z1N; -.
PDBsum; 4ZAO; -.
PDBsum; 4ZWI; -.
PDBsum; 4ZWX; -.
PDBsum; 4ZWY; -.
PDBsum; 4ZWZ; -.
PDBsum; 4ZX0; -.
PDBsum; 4ZX1; -.
PDBsum; 5A6H; -.
PDBsum; 5AMD; -.
PDBsum; 5AMG; -.
PDBsum; 5AML; -.
PDBsum; 5BNL; -.
PDBsum; 5BRU; -.
PDBsum; 5BRV; -.
PDBsum; 5BRW; -.
PDBsum; 5BYI; -.
PDBsum; 5C8I; -.
PDBsum; 5CA2; -.
PDBsum; 5CAC; -.
PDBsum; 5CJL; -.
PDBsum; 5CLU; -.
PDBsum; 5DOG; -.
PDBsum; 5DOH; -.
PDBsum; 5DRS; -.
PDBsum; 5DSI; -.
PDBsum; 5DSJ; -.
PDBsum; 5DSK; -.
PDBsum; 5DSL; -.
PDBsum; 5DSM; -.
PDBsum; 5DSN; -.
PDBsum; 5DSO; -.
PDBsum; 5DSP; -.
PDBsum; 5DSQ; -.
PDBsum; 5DSR; -.
PDBsum; 5E28; -.
PDBsum; 5E2K; -.
PDBsum; 5E2R; -.
PDBsum; 5E2S; -.
PDBsum; 5EH5; -.
PDBsum; 5EH7; -.
PDBsum; 5EH8; -.
PDBsum; 5EHE; -.
PDBsum; 5EHV; -.
PDBsum; 5EHW; -.
PDBsum; 5EIJ; -.
PDBsum; 5EKH; -.
PDBsum; 5EKJ; -.
PDBsum; 5EKM; -.
PDBsum; 5EOI; -.
PDBsum; 5FDC; -.
PDBsum; 5FDI; -.
PDBsum; 5FLO; -.
PDBsum; 5FLP; -.
PDBsum; 5FLQ; -.
PDBsum; 5FLR; -.
PDBsum; 5FLS; -.
PDBsum; 5FLT; -.
PDBsum; 5FNG; -.
PDBsum; 5FNH; -.
PDBsum; 5FNI; -.
PDBsum; 5FNJ; -.
PDBsum; 5FNK; -.
PDBsum; 5FNL; -.
PDBsum; 5FNM; -.
PDBsum; 5G01; -.
PDBsum; 5G03; -.
PDBsum; 5G0B; -.
PDBsum; 5G0C; -.
PDBsum; 5GMN; -.
PDBsum; 5J8Z; -.
PDBsum; 5JDV; -.
PDBsum; 5JE7; -.
PDBsum; 5JEG; -.
PDBsum; 5JEH; -.
PDBsum; 5JEP; -.
PDBsum; 5JES; -.
PDBsum; 5JG3; -.
PDBsum; 5JG5; -.
PDBsum; 5JGS; -.
PDBsum; 5JGT; -.
PDBsum; 5JMZ; -.
PDBsum; 5JN1; -.
PDBsum; 5JN3; -.
PDBsum; 5JN7; -.
PDBsum; 5JQ0; -.
PDBsum; 5JQT; -.
PDBsum; 5L3O; -.
PDBsum; 5L6K; -.
PDBsum; 5L6T; -.
PDBsum; 5L70; -.
PDBsum; 5L9E; -.
PDBsum; 5LJQ; -.
PDBsum; 5LJT; -.
PDBsum; 5LL4; -.
PDBsum; 5LL8; -.
PDBsum; 5LLC; -.
PDBsum; 5LLE; -.
PDBsum; 5LLG; -.
PDBsum; 5LLH; -.
PDBsum; 5LMD; -.
PDBsum; 5LVS; -.
PDBsum; 5N0D; -.
PDBsum; 5N0E; -.
PDBsum; 5O07; -.
PDBsum; 5SZ0; -.
PDBsum; 5SZ1; -.
PDBsum; 5SZ2; -.
PDBsum; 5SZ3; -.
PDBsum; 5SZ4; -.
PDBsum; 5SZ5; -.
PDBsum; 5SZ6; -.
PDBsum; 5SZ7; -.
PDBsum; 5T71; -.
PDBsum; 5T72; -.
PDBsum; 5T74; -.
PDBsum; 5T75; -.
PDBsum; 5TFX; -.
PDBsum; 5TH4; -.
PDBsum; 5THI; -.
PDBsum; 5THJ; -.
PDBsum; 5THN; -.
PDBsum; 5TI0; -.
PDBsum; 5TXY; -.
PDBsum; 5TY1; -.
PDBsum; 5TY8; -.
PDBsum; 5TY9; -.
PDBsum; 5TYA; -.
PDBsum; 5U0D; -.
PDBsum; 5U0E; -.
PDBsum; 5U0F; -.
PDBsum; 5U0G; -.
PDBsum; 5ULN; -.
PDBsum; 5VGY; -.
PDBsum; 5WEX; -.
PDBsum; 6CA2; -.
PDBsum; 7CA2; -.
PDBsum; 8CA2; -.
PDBsum; 9CA2; -.
ProteinModelPortal; P00918; -.
SMR; P00918; -.
BioGrid; 107215; 14.
IntAct; P00918; 6.
MINT; MINT-1367766; -.
STRING; 9606.ENSP00000285379; -.
BindingDB; P00918; -.
ChEMBL; CHEMBL205; -.
DrugBank; DB03333; (4-sulfamoyl-phenyl)-thiocarbamic acid O-(2-thiophen-3-yl-ethyl) ester.
DrugBank; DB02479; (R)-N-(3-Indol-1-Yl-2-Methyl-Propyl)-4-Sulfamoyl-Benzamide.
DrugBank; DB03950; (S)-N-(3-Indol-1-Yl-2-Methyl-Propyl)-4-Sulfamoyl-Benzamide.
DrugBank; DB08659; 2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide.
DrugBank; DB08046; 2-chloro-5-[(1S)-1-hydroxy-3-oxo-2H-isoindol-1-yl]benzenesulfonamide.
DrugBank; DB08156; 3-[4-(AMINOSULFONYL)PHENYL]PROPANOIC ACID.
DrugBank; DB04203; 3-Mercuri-4-Aminobenzenesulfonamide.
DrugBank; DB04394; 3-Nitro-4-(2-Oxo-Pyrrolidin-1-Yl)-Benzenesulfonamide.
DrugBank; DB08782; 4-(2-AMINOETHYL)BENZENESULFONAMIDE.
DrugBank; DB02429; 4-(Aminosulfonyl)-N-[(4-Fluorophenyl)Methyl]-Benzamide.
DrugBank; DB01671; 4-(Hydroxymercury)Benzoic Acid.
DrugBank; DB08202; 4-({[(4-METHYLPIPERAZIN-1-YL)AMINO]CARBONOTHIOYL}AMINO)BENZENESULFONAMIDE.
DrugBank; DB01784; 4-Flourobenzenesulfonamide.
DrugBank; DB03385; 4-Methylimidazole.
DrugBank; DB03697; 4-Sulfonamide-[1-(4-Aminobutane)]Benzamide.
DrugBank; DB04002; 4-Sulfonamide-[4-(Thiomethylaminobutane)]Benzamide.
DrugBank; DB00819; Acetazolamide.
DrugBank; DB03877; AL4623.
DrugBank; DB04089; AL5300.
DrugBank; DB01964; AL5424.
DrugBank; DB03526; AL5927.
DrugBank; DB04371; AL6528.
DrugBank; DB02220; Al7089a.
DrugBank; DB03221; AL7099A.
DrugBank; DB02602; AL7182.
DrugBank; DB02535; Aminodi(Ethyloxy)Ethylaminocarbonylbenzenesulfonamide.
DrugBank; DB00436; Bendroflumethiazide.
DrugBank; DB00562; Benzthiazide.
DrugBank; DB01194; Brinzolamide.
DrugBank; DB00880; Chlorothiazide.
DrugBank; DB02679; Cyanamide.
DrugBank; DB00606; Cyclothiazide.
DrugBank; DB02866; Dansylamide.
DrugBank; DB01119; Diazoxide.
DrugBank; DB01144; Diclofenamide.
DrugBank; DB00869; Dorzolamide.
DrugBank; DB08846; Ellagic Acid.
DrugBank; DB01031; Ethinamate.
DrugBank; DB00311; Ethoxzolamide.
DrugBank; DB08157; ETHYL 3-[4-(AMINOSULFONYL)PHENYL]PROPANOATE.
DrugBank; DB01942; Formic Acid.
DrugBank; DB00695; Furosemide.
DrugBank; DB00999; Hydrochlorothiazide.
DrugBank; DB00774; Hydroflumethiazide.
DrugBank; DB08165; indane-5-sulfonamide.
DrugBank; DB03975; Mercuribenzoic Acid.
DrugBank; DB00703; Methazolamide.
DrugBank; DB00232; Methyclothiazide.
DrugBank; DB02069; N-(2-Flouro-Benzyl)-4-Sulfamoyl-Benzamide.
DrugBank; DB08301; N-({[4-(AMINOSULFONYL)PHENYL]AMINO}CARBONYL)-4-METHYLBENZENESULFONAMIDE.
DrugBank; DB03596; N-[2-(1h-Indol-5-Yl)-Butyl]-4-Sulfamoyl-Benzamide.
DrugBank; DB07476; N-[4-(AMINOSULFONYL)PHENYL]-2-MERCAPTOBENZAMIDE.
DrugBank; DB01748; N-Benzyl-4-Sulfamoyl-Benzamide.
DrugBank; DB08155; N-{2-[4-(AMINOSULFONYL)PHENYL]ETHYL}ACETAMIDE.
DrugBank; DB07710; PHENYLALANYLAMINODI(ETHYLOXY)ETHYL BENZENESULFONAMIDEAMINOCARBONYLBENZENESULFONAMIDE.
DrugBank; DB01325; Quinethazone.
DrugBank; DB09460; Sodium carbonate.
DrugBank; DB08329; SULTHIAME.
DrugBank; DB00273; Topiramate.
DrugBank; DB01021; Trichlormethiazide.
DrugBank; DB03904; Urea.
DrugBank; DB00909; Zonisamide.
iPTMnet; P00918; -.
PhosphoSitePlus; P00918; -.
BioMuta; CA2; -.
OGP; P00918; -.
REPRODUCTION-2DPAGE; IPI00218414; -.
REPRODUCTION-2DPAGE; P00918; -.
UCD-2DPAGE; P00918; -.
EPD; P00918; -.
PaxDb; P00918; -.
PeptideAtlas; P00918; -.
PRIDE; P00918; -.
DNASU; 760; -.
Ensembl; ENST00000285379; ENSP00000285379; ENSG00000104267.
GeneID; 760; -.
KEGG; hsa:760; -.
CTD; 760; -.
DisGeNET; 760; -.
EuPathDB; HostDB:ENSG00000104267.9; -.
GeneCards; CA2; -.
HGNC; HGNC:1373; CA2.
HPA; CAB010102; -.
HPA; HPA001550; -.
MalaCards; CA2; -.
MIM; 259730; phenotype.
MIM; 611492; gene.
neXtProt; NX_P00918; -.
OpenTargets; ENSG00000104267; -.
Orphanet; 2785; Osteopetrosis with renal tubular acidosis.
PharmGKB; PA25989; -.
eggNOG; KOG0382; Eukaryota.
eggNOG; COG3338; LUCA.
GeneTree; ENSGT00760000118915; -.
HOGENOM; HOG000112637; -.
HOVERGEN; HBG002837; -.
InParanoid; P00918; -.
KO; K18245; -.
OMA; HTVDKKK; -.
OrthoDB; EOG091G0XFM; -.
PhylomeDB; P00918; -.
TreeFam; TF316425; -.
BRENDA; 4.2.1.1; 2681.
Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
SABIO-RK; P00918; -.
ChiTaRS; CA2; human.
EvolutionaryTrace; P00918; -.
GeneWiki; Carbonic_anhydrase_II; -.
GenomeRNAi; 760; -.
PRO; PR:P00918; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104267; -.
CleanEx; HS_CA2; -.
ExpressionAtlas; P00918; baseline and differential.
Genevisible; P00918; HS.
GO; GO:0045177; C:apical part of cell; HTP:UniProtKB.
GO; GO:0030424; C:axon; RCA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; RCA:Ensembl.
GO; GO:0005737; C:cytoplasm; HTP:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:Reactome.
GO; GO:0070062; C:extracellular exosome; HTP:UniProtKB.
GO; GO:0005902; C:microvillus; RCA:Ensembl.
GO; GO:0043209; C:myelin sheath; RCA:Ensembl.
GO; GO:0005886; C:plasma membrane; HTP:UniProtKB.
GO; GO:0004064; F:arylesterase activity; HDA:CACAO.
GO; GO:0004089; F:carbonate dehydratase activity; HDA:CACAO.
GO; GO:0008270; F:zinc ion binding; HTP:UniProtKB.
GO; GO:0038166; P:angiotensin-activated signaling pathway; HTP:UniProtKB.
GO; GO:0015701; P:bicarbonate transport; IBA:Reactome.
GO; GO:0015670; P:carbon dioxide transport; RCA:Ensembl.
GO; GO:0071498; P:cellular response to fluid shear stress; RCA:Ensembl.
GO; GO:0001822; P:kidney development; RCA:Ensembl.
GO; GO:0002009; P:morphogenesis of an epithelium; RCA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; RCA:Ensembl.
GO; GO:0006730; P:one-carbon metabolic process; RCA:InterPro.
GO; GO:0045780; P:positive regulation of bone resorption; RCA:Ensembl.
GO; GO:0032849; P:positive regulation of cellular pH reduction; RCA:Ensembl.
GO; GO:2001150; P:positive regulation of dipeptide transmembrane transport; HMP:UniProtKB.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; RCA:Ensembl.
GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; RCA:Ensembl.
GO; GO:0044070; P:regulation of anion transport; HTP:UniProtKB.
GO; GO:2001225; P:regulation of chloride transport; RCA:Ensembl.
GO; GO:0051453; P:regulation of intracellular pH; HMP:UniProtKB.
GO; GO:0043627; P:response to estrogen; RCA:Ensembl.
GO; GO:0009268; P:response to pH; RCA:Ensembl.
GO; GO:0048545; P:response to steroid hormone; RCA:Ensembl.
GO; GO:0010043; P:response to zinc ion; RCA:Ensembl.
GO; GO:0046903; P:secretion; RCA:Ensembl.
Gene3D; 3.10.200.10; -; 1.
InterPro; IPR001148; Carbonic_anhydrase_a.
InterPro; IPR023561; Carbonic_anhydrase_a-class.
InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
InterPro; IPR036398; Carbonic_anhydrase_a_sf.
PANTHER; PTHR18952; PTHR18952; 1.
Pfam; PF00194; Carb_anhydrase; 1.
SMART; SM01057; Carb_anhydrase; 1.
SUPFAM; SSF51069; SSF51069; 1.
PROSITE; PS00162; ALPHA_CA_1; 1.
PROSITE; PS51144; ALPHA_CA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell membrane; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation; Lyase;
Membrane; Metal-binding; Osteopetrosis; Phosphoprotein; Polymorphism;
Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:4207120,
ECO:0000269|PubMed:823150}.
CHAIN 2 260 Carbonic anhydrase 2.
/FTId=PRO_0000077418.
DOMAIN 3 259 Alpha-carbonic anhydrase.
{ECO:0000270|PROSITE-ProRule:PRU01134}.
REGION 198 199 Substrate binding.
{ECO:0000269|PubMed:10550681,
ECO:0000269|PubMed:19520834}.
ACT_SITE 64 64 Proton acceptor.
{ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:19170619}.
ACT_SITE 67 67 {ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:19170619}.
ACT_SITE 127 127 {ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:19170619}.
METAL 94 94 Zinc; catalytic.
{ECO:0000269|PubMed:11076507,
ECO:0000269|PubMed:12499545,
ECO:0000269|PubMed:1336460,
ECO:0000269|PubMed:1433293,
ECO:0000269|PubMed:1909891,
ECO:0000269|PubMed:19583303,
ECO:0000269|PubMed:3151019,
ECO:0000269|PubMed:3151020,
ECO:0000269|PubMed:4621826,
ECO:0000269|PubMed:7761440,
ECO:0000269|PubMed:7803386,
ECO:0000269|PubMed:7901850,
ECO:0000269|PubMed:8218160,
ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:8331673,
ECO:0000269|PubMed:8399159,
ECO:0000269|PubMed:8431430,
ECO:0000269|PubMed:8451242,
ECO:0000269|PubMed:8482389,
ECO:0000269|PubMed:8639494,
ECO:0000269|PubMed:8987974,
ECO:0000269|PubMed:9398308,
ECO:0000269|PubMed:9865942}.
METAL 96 96 Zinc; catalytic.
{ECO:0000269|PubMed:11076507,
ECO:0000269|PubMed:12499545,
ECO:0000269|PubMed:1336460,
ECO:0000269|PubMed:1433293,
ECO:0000269|PubMed:1909891,
ECO:0000269|PubMed:19583303,
ECO:0000269|PubMed:3151019,
ECO:0000269|PubMed:3151020,
ECO:0000269|PubMed:7761440,
ECO:0000269|PubMed:7803386,
ECO:0000269|PubMed:7901850,
ECO:0000269|PubMed:8218160,
ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:8331673,
ECO:0000269|PubMed:8399159,
ECO:0000269|PubMed:8431430,
ECO:0000269|PubMed:8451242,
ECO:0000269|PubMed:8482389,
ECO:0000269|PubMed:8639494,
ECO:0000269|PubMed:8987974,
ECO:0000269|PubMed:9398308,
ECO:0000269|PubMed:9865942}.
METAL 119 119 Zinc; catalytic.
{ECO:0000269|PubMed:11076507,
ECO:0000269|PubMed:12499545,
ECO:0000269|PubMed:1336460,
ECO:0000269|PubMed:1433293,
ECO:0000269|PubMed:1909891,
ECO:0000269|PubMed:19583303,
ECO:0000269|PubMed:3151019,
ECO:0000269|PubMed:3151020,
ECO:0000269|PubMed:7761440,
ECO:0000269|PubMed:7803386,
ECO:0000269|PubMed:7901850,
ECO:0000269|PubMed:8218160,
ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:8331673,
ECO:0000269|PubMed:8399159,
ECO:0000269|PubMed:8431430,
ECO:0000269|PubMed:8451242,
ECO:0000269|PubMed:8482389,
ECO:0000269|PubMed:8639494,
ECO:0000269|PubMed:8987974,
ECO:0000269|PubMed:9398308,
ECO:0000269|PubMed:9865942}.
BINDING 62 62 Activator. {ECO:0000269|PubMed:16214338,
ECO:0000269|PubMed:17127057,
ECO:0000269|PubMed:9265618}.
BINDING 67 67 Activator. {ECO:0000269|PubMed:16214338,
ECO:0000269|PubMed:17127057,
ECO:0000269|PubMed:9265618}.
BINDING 92 92 Activator. {ECO:0000269|PubMed:16214338,
ECO:0000269|PubMed:17127057,
ECO:0000269|PubMed:9265618}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:4207120,
ECO:0000269|PubMed:823150}.
MOD_RES 2 2 Phosphoserine.
{ECO:0007001|UniProtKB:P27139}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000307|PubMed:24275569}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000307|PubMed:24275569}.
VARIANT 18 18 K -> E (in Jogjakarta;
dbSNP:rs118203931).
{ECO:0000269|PubMed:6817747}.
/FTId=VAR_001380.
VARIANT 92 92 Q -> P (in OPTB3; in Czechoslovakia).
{ECO:0000269|PubMed:15300855,
ECO:0000269|PubMed:9143915}.
/FTId=VAR_001381.
VARIANT 94 94 H -> Y (in OPTB3; partial loss of
activity). {ECO:0000269|PubMed:15300855}.
/FTId=VAR_021009.
VARIANT 107 107 H -> Y (in OPTB3; frequent mutation;
dbSNP:rs118203933).
{ECO:0000269|PubMed:15300855,
ECO:0000269|PubMed:1542674,
ECO:0000269|PubMed:1928091,
ECO:0000269|PubMed:8834238}.
/FTId=VAR_001382.
VARIANT 144 144 G -> R (in OPTB3; complete loss of
activity). {ECO:0000269|PubMed:15300855}.
/FTId=VAR_021010.
VARIANT 236 236 P -> H (in Melbourne; dbSNP:rs118203932).
{ECO:0000269|PubMed:6407977}.
/FTId=VAR_001383.
VARIANT 252 252 N -> D (in dbSNP:rs2228063).
/FTId=VAR_001384.
MUTAGEN 5 5 W->A: Impaired activity, not rescued by
4-methylimidazole (4-MI); when associated
with W-64. {ECO:0000269|PubMed:17071654}.
MUTAGEN 7 7 Y->F: Enhanced activity.
{ECO:0000269|PubMed:12171926,
ECO:0000269|PubMed:17330962}.
MUTAGEN 7 7 Y->H: Reduced proton transfer rate.
{ECO:0000269|PubMed:12171926,
ECO:0000269|PubMed:17330962}.
MUTAGEN 62 62 N->A: Reduced activity.
{ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:18942852}.
MUTAGEN 62 62 N->D: Strongly reduced activity.
{ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:18942852}.
MUTAGEN 62 62 N->H: Reduced proton transfer; when
associated with A-64.
{ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:18942852}.
MUTAGEN 62 62 N->L: Reduced activity.
{ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:18942852}.
MUTAGEN 62 62 N->T: Reduced activity.
{ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:18942852}.
MUTAGEN 62 62 N->V: Reduced activity.
{ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:18942852}.
MUTAGEN 64 64 H->A: Reduced CO(2) hydrase activity,
rescued by 4-methylimidazole (4-MI).
Reduced proton transfer; when associated
with H-62. Enhanced proton transfer; when
associated with H-67. Enhanced proton
transfer capacity; when associated with
H-99. {ECO:0000269|PubMed:11327835,
ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:16106378,
ECO:0000269|PubMed:17071654}.
MUTAGEN 64 64 H->G: Impaired activity, not rescued by
4-methylimidazole (4-MI).
{ECO:0000269|PubMed:11327835,
ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:16106378,
ECO:0000269|PubMed:17071654}.
MUTAGEN 64 64 H->W: Impaired activity, rescued by 4-
methylimidazole (4-MI). Impaired
activity, not rescued by 4-
methylimidazole (4-MI); when associated
with A-5. {ECO:0000269|PubMed:11327835,
ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:16106378,
ECO:0000269|PubMed:17071654}.
MUTAGEN 65 65 A->F: Reduced activity.
{ECO:0000269|PubMed:19170619}.
MUTAGEN 65 65 A->H,L,S: Normal activity.
{ECO:0000269|PubMed:19170619}.
MUTAGEN 67 67 N->H: Enhanced proton transfer; when
associated with A-64.
{ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:19170619}.
MUTAGEN 67 67 N->L: Reduced activity.
{ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:19170619}.
MUTAGEN 67 67 N->Q: Normal activity.
{ECO:0000269|PubMed:15667203,
ECO:0000269|PubMed:17330962,
ECO:0000269|PubMed:19170619}.
MUTAGEN 94 94 H->C,D,E,N,Q: Strongly reduced CO(2)
hydrase and p-nitrophenyl acetate
esterase activities, impaired stability
of zinc binding.
{ECO:0000269|PubMed:8431430,
ECO:0000269|PubMed:9398308}.
MUTAGEN 106 106 E->A,Q: Strongly reduced CO(2) hydrase
activity. {ECO:0000269|PubMed:15299482,
ECO:0000269|PubMed:7901850}.
MUTAGEN 106 106 E->D: Normal CO(2) hydrase activity.
{ECO:0000269|PubMed:15299482,
ECO:0000269|PubMed:7901850}.
MUTAGEN 117 117 E->Q: Strongly reduced activity and
sulfonamide affinity.
{ECO:0000269|PubMed:8639494}.
MUTAGEN 119 119 H->D,N,Q: Reduced activity.
{ECO:0000269|PubMed:9398308}.
MUTAGEN 119 119 H->E: Strongly reduced activity.
{ECO:0000269|PubMed:9398308}.
MUTAGEN 121 121 V->A,G,I,L,S: Reduced CO(2) hydrase and
p-nitrophenyl acetate esterase
activities. {ECO:0000269|PubMed:1910042}.
MUTAGEN 121 121 V->K,R: Strongly reduced CO(2) hydrase
and p-nitrophenyl acetate esterase
activities. {ECO:0000269|PubMed:1910042}.
MUTAGEN 142 142 V->F,Y: Strongly impaired activity.
{ECO:0000269|PubMed:1932029}.
MUTAGEN 142 142 V->G: Weakly impaired activity.
{ECO:0000269|PubMed:1932029}.
MUTAGEN 142 142 V->H: Impaired activity.
{ECO:0000269|PubMed:1932029}.
MUTAGEN 197 197 L->A: Reduced CO(2) hydrase activity.
{ECO:0000269|PubMed:8485129}.
MUTAGEN 197 197 L->E,H,R: Strongly reduced CO(2) hydrase
activity. {ECO:0000269|PubMed:8485129}.
MUTAGEN 197 197 L->F: Normal activity.
{ECO:0000269|PubMed:8485129}.
MUTAGEN 198 198 T->A,C,H,P: Strongly reduced activity.
{ECO:0000269|PubMed:12056894,
ECO:0000269|PubMed:7761440,
ECO:0000269|PubMed:7901850,
ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:8399159}.
MUTAGEN 198 198 T->D,E: Strongly reduced activity, but
enhanced zinc affinity.
{ECO:0000269|PubMed:12056894,
ECO:0000269|PubMed:7761440,
ECO:0000269|PubMed:7901850,
ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:8399159}.
MUTAGEN 198 198 T->S,V: Reduced activity.
{ECO:0000269|PubMed:12056894,
ECO:0000269|PubMed:7761440,
ECO:0000269|PubMed:7901850,
ECO:0000269|PubMed:8262987,
ECO:0000269|PubMed:8399159}.
MUTAGEN 199 199 T->H: Higher affinity for bicarbonate.
Enhanced proton transfer capacity; when
associated with A-64.
{ECO:0000269|PubMed:16106378,
ECO:0000269|PubMed:1909891,
ECO:0000269|PubMed:8451242}.
MUTAGEN 199 199 T->S: Enhanced p-nitrophenyl acetate
esterase activity, but normal CO(2)
hydrase activity.
{ECO:0000269|PubMed:16106378,
ECO:0000269|PubMed:1909891,
ECO:0000269|PubMed:8451242}.
MUTAGEN 201 201 P->A: Normal CO(2) hydrase activity, but
impaired stability.
{ECO:0000269|PubMed:8218160}.
CONFLICT 179 180 DP -> AA (in Ref. 6; AAH11949).
{ECO:0000320}.
TURN 9 11 {ECO:0000307|PDB:3K34}.
TURN 13 15 {ECO:0000307|PDB:3K34}.
HELIX 16 18 {ECO:0000307|PDB:3K34}.
HELIX 21 24 {ECO:0000307|PDB:3K34}.
STRAND 25 27 {ECO:0000307|PDB:3K34}.
STRAND 31 33 {ECO:0000307|PDB:2X7S}.
TURN 35 37 {ECO:0000307|PDB:3K34}.
STRAND 38 40 {ECO:0000307|PDB:3KS3}.
STRAND 42 44 {ECO:0000307|PDB:3KOI}.
STRAND 45 50 {ECO:0000307|PDB:3K34}.
STRAND 56 61 {ECO:0000307|PDB:3K34}.
STRAND 63 70 {ECO:0000307|PDB:3K34}.
STRAND 73 75 {ECO:0000307|PDB:3K34}.
STRAND 77 82 {ECO:0000307|PDB:3K34}.
TURN 83 85 {ECO:0000307|PDB:5GMN}.
STRAND 88 97 {ECO:0000307|PDB:3K34}.
STRAND 106 109 {ECO:0000307|PDB:3K34}.
STRAND 115 124 {ECO:0000307|PDB:3K34}.
HELIX 125 127 {ECO:0000307|PDB:3K34}.
HELIX 130 133 {ECO:0000307|PDB:3K34}.
STRAND 139 151 {ECO:0000307|PDB:3K34}.
HELIX 154 156 {ECO:0000307|PDB:3K34}.
HELIX 157 162 {ECO:0000307|PDB:3K34}.
HELIX 163 165 {ECO:0000307|PDB:3K34}.
STRAND 172 174 {ECO:0000307|PDB:3K34}.
HELIX 180 183 {ECO:0000307|PDB:3K34}.
STRAND 190 195 {ECO:0000307|PDB:3K34}.
STRAND 206 213 {ECO:0000307|PDB:3K34}.
STRAND 215 217 {ECO:0000307|PDB:3K34}.
HELIX 219 225 {ECO:0000307|PDB:3K34}.
TURN 226 228 {ECO:0000307|PDB:4QK3}.
STRAND 229 231 {ECO:0000307|PDB:3K34}.
STRAND 233 235 {ECO:0000307|PDB:4Q06}.
STRAND 256 258 {ECO:0000307|PDB:3K34}.
SEQUENCE 260 AA; 29246 MW; 2EC2BB7548F10558 CRC64;
MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS YDQATSLRIL
NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL DGQGSEHTVD KKKYAAELHL
VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG SAKPGLQKVV DVLDSIKTKG KSADFTNFDP
RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM
VDNWRPAQPL KNRQIKASFK


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EIAAB05175 CA6,Carbonate dehydratase VI,Carbonic anhydrase 6,Carbonic anhydrase VI,CA-VI,Homo sapiens,Human,Salivary carbonic anhydrase,Secreted carbonic anhydrase
EIAAB05176 Ca6,Car6,Carbonate dehydratase VI,Carbonic anhydrase 6,Carbonic anhydrase VI,CA-VI,Mouse,Mus musculus,Salivary carbonic anhydrase,Secreted carbonic anhydrase
EIAAB05177 Bos taurus,Bovine,CA6,Carbonate dehydratase VI,Carbonic anhydrase 6,Carbonic anhydrase VI,CA-VI,Salivary carbonic anhydrase,Secreted carbonic anhydrase
E1799h ELISA CA1,CAB,CA-I,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase B,Carbonic anhydrase I,Homo sapiens,Human 96T
E1799h ELISA kit CA1,CAB,CA-I,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase B,Carbonic anhydrase I,Homo sapiens,Human 96T
E0782h ELISA CA2,CAC,CA-II,Carbonate dehydratase II,Carbonic anhydrase 2,Carbonic anhydrase C,Carbonic anhydrase II,Homo sapiens,Human 96T
E0782h ELISA kit CA2,CAC,CA-II,Carbonate dehydratase II,Carbonic anhydrase 2,Carbonic anhydrase C,Carbonic anhydrase II,Homo sapiens,Human 96T
U0782h CLIA CA2,CAC,CA-II,Carbonate dehydratase II,Carbonic anhydrase 2,Carbonic anhydrase C,Carbonic anhydrase II,Homo sapiens,Human 96T
U1799h CLIA kit CA1,CAB,CA-I,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase B,Carbonic anhydrase I,Homo sapiens,Human 96T
U1799h CLIA CA1,CAB,CA-I,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase B,Carbonic anhydrase I,Homo sapiens,Human 96T
EIAAB05150 CA12,Carbonate dehydratase XII,Carbonic anhydrase 12,Carbonic anhydrase XII,CA-XII,Homo sapiens,Human,Tumor antigen HOM-RCC-3.1.3
EIAAB05170 CA Y,Ca5,Ca5a,Car5,Car5a,Carbonate dehydratase VA,Carbonic anhydrase 5A, mitochondrial,Carbonic anhydrase VA,CA-VA,Mouse,Mus musculus
EIAAB05183 Ca9,CAIX,CA-IX,Car9,Carbonate dehydratase IX,Carbonic anhydrase 9,Carbonic anhydrase IX,Membrane antigen MN homolog,Mouse,Mus musculus
EIAAB05155 Ca14,Car14,Carbonate dehydratase XIV,Carbonic anhydrase 14,Carbonic anhydrase XIV,Catm,CA-XIV,Mouse,Mus musculus
EIAAB05169 CA5,CA5A,Carbonate dehydratase VA,Carbonic anhydrase 5A, mitochondrial,Carbonic anhydrase VA,CA-VA,Homo sapiens,Human
EIAAB05156 CA14,Carbonate dehydratase XIV,Carbonic anhydrase 14,Carbonic anhydrase XIV,CA-XIV,Homo sapiens,Human,UNQ690_PRO1335
EIAAB05171 Ca5b,Car5b,Carbonate dehydratase VB,Carbonic anhydrase 5B, mitochondrial,Carbonic anhydrase VB,CA-VB,Mouse,Mus musculus
EIAAB05172 Ca5b,Car5b,Carbonate dehydratase VB,Carbonic anhydrase 5B, mitochondrial,Carbonic anhydrase VB,CA-VB,Rat,Rattus norvegicus
EIAAB05173 CA5B,Carbonate dehydratase VB,Carbonic anhydrase 5B, mitochondrial,Carbonic anhydrase VB,CA-VB,Homo sapiens,Human
U1799Rb CLIA kit CA1,CA-I,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase I,Oryctolagus cuniculus,Rabbit 96T
U1799r CLIA kit Ca1,CA-I,Car1,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase I,Rat,Rattus norvegicus 96T
E1799m ELISA kit Ca1,CA-I,Car1,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase I,Mouse,Mus musculus 96T
E1799Rb ELISA kit CA1,CA-I,Carbonate dehydratase I,Carbonic anhydrase 1,Carbonic anhydrase I,Oryctolagus cuniculus,Rabbit 96T
EIAAB05157 Ca15,Car15,Carbonate dehydratase XV,Carbonic anhydrase 15,Carbonic anhydrase XV,CA-XV,Mouse,Mus musculus
EIAAB05151 CA12,Carbonate dehydratase XII,Carbonic anhydrase 12,Carbonic anhydrase XII,CA-XII,Oryctolagus cuniculus,Rabbit


 

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