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DNA polymerase beta (EC 2.7.7.7) (EC 4.2.99.-)

 DPOLB_HUMAN             Reviewed;         335 AA.
P06746; B2RC78; Q3KP48; Q6FI34;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-OCT-2018, entry version 219.
RecName: Full=DNA polymerase beta;
EC=2.7.7.7;
EC=4.2.99.-;
Name=POLB;
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=10648175; DOI=10.1006/prep.1999.1167;
Patterson T.A., Little W., Cheng X., Widen S.G., Kumar A., Beard W.A.,
Wilson S.H.;
"Molecular cloning and high-level expression of human polymerase beta
cDNA and comparison of the purified recombinant human and rat
enzymes.";
Protein Expr. Purif. 18:100-110(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7705833; DOI=10.1007/BF00208961;
Dobashi Y., Kubota Y., Shuin T., Torigoe S., Yao M., Hosaka M.;
"Polymorphisms in the human DNA polymerase beta gene.";
Hum. Genet. 95:389-390(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Skin;
PubMed=7914364; DOI=10.1093/nar/22.14.2719;
Chyan Y.-J., Ackerman S., Shepherd N.S., McBride O.W., Widen S.G.,
Wilson S.H., Wood T.G.;
"The human DNA polymerase beta gene structure. Evidence of alternative
splicing in gene expression.";
Nucleic Acids Res. 22:2719-2725(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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 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.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-242.
NIEHS SNPs program;
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
PubMed=3182828;
Widen S.G., Kedar P., Wilson S.H.;
"Human beta-polymerase gene. Structure of the 5'-flanking region and
active promoter.";
J. Biol. Chem. 263:16992-16998(1988).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-32.
PubMed=3284575; DOI=10.1021/bi00403a010;
Abbotts J., Sengupta D.N., Zmudzka B., Widen S.G., Notario V.,
Wilson S.H.;
"Expression of human DNA polymerase beta in Escherichia coli and
characterization of the recombinant enzyme.";
Biochemistry 27:901-909(1988).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 18-335.
PubMed=2423078; DOI=10.1016/0006-291X(86)90916-2;
Sengupta D.N., Zmudzka B.Z., Kumar P., Cobianchi F., Skowronski J.,
Wilson S.H.;
"Sequence of human DNA polymerase beta mRNA obtained through cDNA
cloning.";
Biochem. Biophys. Res. Commun. 136:341-347(1986).
[11]
FUNCTION, AND INTERACTION WITH APEX1.
PubMed=9207062; DOI=10.1073/pnas.94.14.7166;
Bennett R.A., Wilson D.M. III, Wong D., Demple B.;
"Interaction of human apurinic endonuclease and DNA polymerase beta in
the base excision repair pathway.";
Proc. Natl. Acad. Sci. U.S.A. 94:7166-7169(1997).
[12]
FUNCTION, AND MUTAGENESIS OF LYS-35; TYR-39; LYS-68; LYS-72 AND
LYS-84.
PubMed=9572863; DOI=10.1021/bi9727545;
Matsumoto Y., Kim K., Katz D.S., Feng J.-A.;
"Catalytic center of DNA polymerase beta for excision of deoxyribose
phosphate groups.";
Biochemistry 37:6456-6464(1998).
[13]
FUNCTION.
PubMed=11805079; DOI=10.1074/jbc.C100577200;
DeMott M.S., Beyret E., Wong D., Bales B.C., Hwang J.-T.,
Greenberg M.M., Demple B.;
"Covalent trapping of human DNA polymerase beta by the oxidative DNA
lesion 2-deoxyribonolactone.";
J. Biol. Chem. 277:7637-7640(2002).
[14]
METHYLATION AT ARG-83 AND ARG-152 BY PRMT6, AND MUTAGENESIS OF ARG-83
AND ARG-152.
PubMed=16600869; DOI=10.1016/j.molcel.2006.02.013;
El-Andaloussi N., Valovka T., Toueille M., Steinacher R., Focke F.,
Gehrig P., Covic M., Hassa P.O., Schaer P., Huebscher U.,
Hottiger M.O.;
"Arginine methylation regulates DNA polymerase beta.";
Mol. Cell 22:51-62(2006).
[15]
SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-41; LYS-61 AND LYS-81, AND
MUTAGENESIS OF LYS-41; LYS-61 AND LYS-81.
PubMed=19713937; DOI=10.1038/emboj.2009.243;
Parsons J.L., Tait P.S., Finch D., Dianova I.I., Edelmann M.J.,
Khoronenkova S.V., Kessler B.M., Sharma R.A., McKenna W.G.,
Dianov G.L.;
"Ubiquitin ligase ARF-BP1/Mule modulates base excision repair.";
EMBO J. 28:3207-3215(2009).
[16]
FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-41; LYS-61 AND
LYS-81, DEUBIQUITINATION BY USP47, AND INTERACTION WITH USP47.
PubMed=21362556; DOI=10.1016/j.molcel.2011.02.016;
Parsons J.L., Dianova I.I., Khoronenkova S.V., Edelmann M.J.,
Kessler B.M., Dianov G.L.;
"USP47 is a deubiquitylating enzyme that regulates base excision
repair by controlling steady-state levels of DNA Polymerase beta.";
Mol. Cell 41:609-615(2011).
[17]
INTERACTS WITH FAM168A.
PubMed=25260657; DOI=10.1007/s11010-014-2217-x;
Liu X., Wang C., Gu Y., Zhang Z., Zheng G., He Z.;
"TCRP1 contributes to cisplatin resistance by preventing Pol beta
degradation in lung cancer cells.";
Mol. Cell. Biochem. 398:175-183(2015).
[18]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH DNA; ATP AND
METAL IONS.
PubMed=8841119; DOI=10.1021/bi9529566;
Pelletier H., Sawaya M.R., Wolfle W., Wilson S.H., Kraut J.;
"A structural basis for metal ion mutagenicity and nucleotide
selectivity in human DNA polymerase beta.";
Biochemistry 35:12762-12777(1996).
[19]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH DNA AND METAL
IONS.
PubMed=8841120; DOI=10.1021/bi960790i;
Pelletier H., Sawaya M.R.;
"Characterization of the metal ion binding helix-hairpin-helix motifs
in human DNA polymerase beta by X-ray structural analysis.";
Biochemistry 35:12778-12787(1996).
[20]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH DNA.
PubMed=9287163; DOI=10.1021/bi9703812;
Sawaya M.R., Prasad R., Wilson S.H., Kraut J., Pelletier H.;
"Crystal structures of human DNA polymerase beta complexed with gapped
and nicked DNA: evidence for an induced fit mechanism.";
Biochemistry 36:11205-11215(1997).
[21]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH DNA.
PubMed=12517346; DOI=10.1016/S0969-2126(02)00930-9;
Krahn J.M., Beard W.A., Miller H., Grollman A.P., Wilson S.H.;
"Structure of DNA polymerase beta with the mutagenic DNA lesion 8-
oxodeoxyguanine reveals structural insights into its coding
potential.";
Structure 11:121-127(2003).
-!- FUNCTION: Repair polymerase that plays a key role in base-excision
repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity
that removes the 5' sugar phosphate and also acts as a DNA
polymerase that adds one nucleotide to the 3' end of the arising
single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a
stepwise distributive fashion rather than in a processive fashion
as for other DNA polymerases. {ECO:0000269|PubMed:11805079,
ECO:0000269|PubMed:21362556, ECO:0000269|PubMed:9207062,
ECO:0000269|PubMed:9572863}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
-!- SUBUNIT: Monomer. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP
and USP47. Interacts with FAM168A (PubMed:25260657).
{ECO:0000269|PubMed:12517346, ECO:0000269|PubMed:21362556,
ECO:0000269|PubMed:25260657, ECO:0000269|PubMed:8841119,
ECO:0000269|PubMed:8841120, ECO:0000269|PubMed:9207062,
ECO:0000269|PubMed:9287163}.
-!- INTERACTION:
Q9H5J8:TAF1D; NbExp=4; IntAct=EBI-713836, EBI-716128;
P29144:TPP2; NbExp=6; IntAct=EBI-713836, EBI-1044672;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Cytoplasmic in
normal conditions. Translocates to the nucleus following DNA
damage.
-!- DOMAIN: Residues 239-252 form a flexible loop which appears to
affect the polymerase fidelity. {ECO:0000250}.
-!- PTM: Methylation by PRMT6 stimulates the polymerase activity by
enhancing DNA binding and processivity.
{ECO:0000269|PubMed:16600869}.
-!- PTM: Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated
by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of
STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin,
leading to degradation by the proteasome. USP47 mediates the
deubiquitination of monoubiquitinated protein, preventing
polyubiquitination by STUB1/CHIP and its subsequent degradation.
{ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:21362556}.
-!- SIMILARITY: Belongs to the DNA polymerase type-X family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/polb/";
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EMBL; L11607; AAB59441.1; -; mRNA.
EMBL; D29013; BAA06099.1; -; mRNA.
EMBL; U10526; AAB60688.1; -; Genomic_DNA.
EMBL; U10516; AAB60688.1; JOINED; Genomic_DNA.
EMBL; U10517; AAB60688.1; JOINED; Genomic_DNA.
EMBL; U10519; AAB60688.1; JOINED; Genomic_DNA.
EMBL; U10520; AAB60688.1; JOINED; Genomic_DNA.
EMBL; U10521; AAB60688.1; JOINED; Genomic_DNA.
EMBL; U10522; AAB60688.1; JOINED; Genomic_DNA.
EMBL; U10523; AAB60688.1; JOINED; Genomic_DNA.
EMBL; U10524; AAB60688.1; JOINED; Genomic_DNA.
EMBL; U10525; AAB60688.1; JOINED; Genomic_DNA.
EMBL; AK314976; BAG37475.1; -; mRNA.
EMBL; CR536503; CAG38741.1; -; mRNA.
EMBL; CR541802; CAG46601.1; -; mRNA.
EMBL; AF491812; AAL91594.1; -; Genomic_DNA.
EMBL; BC100288; AAI00289.1; -; mRNA.
EMBL; BC106909; AAI06910.1; -; mRNA.
EMBL; J04201; AAA60134.1; -; Genomic_DNA.
EMBL; M13140; AAA60133.1; -; mRNA.
CCDS; CCDS6129.1; -.
PIR; I55273; I55273.
PIR; S48061; S48061.
RefSeq; NP_002681.1; NM_002690.2.
UniGene; Hs.654484; -.
UniGene; Hs.661106; -.
PDB; 1BPX; X-ray; 2.40 A; A=1-335.
PDB; 1BPY; X-ray; 2.20 A; A=1-335.
PDB; 1BPZ; X-ray; 2.60 A; A=1-335.
PDB; 1MQ2; X-ray; 3.10 A; A=1-335.
PDB; 1MQ3; X-ray; 2.80 A; A=1-335.
PDB; 1TV9; X-ray; 2.00 A; A=1-335.
PDB; 1TVA; X-ray; 2.60 A; A=1-335.
PDB; 1ZJM; X-ray; 2.10 A; A=1-335.
PDB; 1ZJN; X-ray; 2.61 A; A=1-335.
PDB; 1ZQA; X-ray; 3.20 A; A=1-335.
PDB; 1ZQB; X-ray; 3.20 A; A=1-335.
PDB; 1ZQC; X-ray; 3.20 A; A=1-335.
PDB; 1ZQD; X-ray; 3.50 A; A=1-335.
PDB; 1ZQE; X-ray; 3.70 A; A=1-335.
PDB; 1ZQF; X-ray; 2.90 A; A=1-335.
PDB; 1ZQG; X-ray; 3.10 A; A=1-335.
PDB; 1ZQH; X-ray; 3.10 A; A=1-335.
PDB; 1ZQI; X-ray; 2.70 A; A=1-335.
PDB; 1ZQJ; X-ray; 3.30 A; A=1-335.
PDB; 1ZQK; X-ray; 3.20 A; A=1-335.
PDB; 1ZQL; X-ray; 3.30 A; A=1-335.
PDB; 1ZQM; X-ray; 3.20 A; A=1-335.
PDB; 1ZQN; X-ray; 3.00 A; A=1-335.
PDB; 1ZQO; X-ray; 3.20 A; A=1-335.
PDB; 1ZQP; X-ray; 2.80 A; A=1-335.
PDB; 1ZQQ; X-ray; 3.30 A; A=1-335.
PDB; 1ZQR; X-ray; 3.70 A; A=1-335.
PDB; 1ZQS; X-ray; 3.30 A; A=1-335.
PDB; 1ZQT; X-ray; 3.40 A; A=1-335.
PDB; 2FMP; X-ray; 1.65 A; A=1-335.
PDB; 2FMQ; X-ray; 2.20 A; A=1-335.
PDB; 2FMS; X-ray; 2.00 A; A=1-335.
PDB; 2I9G; X-ray; 2.10 A; A=1-335.
PDB; 2ISO; X-ray; 2.10 A; A=1-335.
PDB; 2ISP; X-ray; 2.20 A; A=1-335.
PDB; 2P66; X-ray; 2.50 A; A=1-335.
PDB; 2PXI; X-ray; 2.10 A; A=1-335.
PDB; 3C2K; X-ray; 2.40 A; A=1-335.
PDB; 3C2L; X-ray; 2.60 A; A=1-335.
PDB; 3C2M; X-ray; 2.15 A; A=1-335.
PDB; 3GDX; X-ray; 2.20 A; A=10-335.
PDB; 3ISB; X-ray; 2.00 A; A=1-335.
PDB; 3ISC; X-ray; 2.00 A; A=1-335.
PDB; 3ISD; X-ray; 2.60 A; A=1-335.
PDB; 3JPN; X-ray; 2.15 A; A=1-335.
PDB; 3JPO; X-ray; 2.00 A; A=1-335.
PDB; 3JPP; X-ray; 2.10 A; A=1-335.
PDB; 3JPQ; X-ray; 1.90 A; A=1-335.
PDB; 3JPR; X-ray; 2.10 A; A=1-335.
PDB; 3JPS; X-ray; 2.00 A; A=1-335.
PDB; 3JPT; X-ray; 2.15 A; A=1-335.
PDB; 3LK9; X-ray; 2.50 A; A=1-335.
PDB; 3MBY; X-ray; 2.00 A; A=1-335.
PDB; 3OGU; X-ray; 1.84 A; A=1-335.
PDB; 3RH4; X-ray; 1.92 A; A=1-335.
PDB; 3RH5; X-ray; 2.10 A; A=1-335.
PDB; 3RH6; X-ray; 2.05 A; A=1-335.
PDB; 3RJE; X-ray; 2.10 A; A=1-335.
PDB; 3RJF; X-ray; 2.30 A; A=1-335.
PDB; 3RJG; X-ray; 2.00 A; A=1-335.
PDB; 3RJH; X-ray; 2.20 A; A=1-335.
PDB; 3RJI; X-ray; 2.30 A; A=1-335.
PDB; 3RJJ; X-ray; 2.00 A; A=1-335.
PDB; 3RJK; X-ray; 2.10 A; A=1-335.
PDB; 3TFR; X-ray; 2.00 A; A=1-335.
PDB; 3TFS; X-ray; 2.00 A; A=1-335.
PDB; 4DO9; X-ray; 2.05 A; A=1-335.
PDB; 4DOA; X-ray; 2.05 A; A=1-335.
PDB; 4DOB; X-ray; 2.05 A; A=1-335.
PDB; 4DOC; X-ray; 1.95 A; A=1-335.
PDB; 4F5N; X-ray; 1.80 A; A=1-335.
PDB; 4F5O; X-ray; 2.00 A; A=1-335.
PDB; 4F5P; X-ray; 1.85 A; A=1-335.
PDB; 4F5Q; X-ray; 2.25 A; A=1-335.
PDB; 4F5R; X-ray; 2.20 A; A/B=1-335.
PDB; 4GXI; X-ray; 1.95 A; A=1-335.
PDB; 4GXJ; X-ray; 2.20 A; A=1-335.
PDB; 4GXK; X-ray; 2.00 A; A=1-335.
PDB; 4JWM; X-ray; 2.00 A; A=1-335.
PDB; 4JWN; X-ray; 2.39 A; A=1-335.
PDB; 4KLD; X-ray; 1.92 A; A=1-335.
PDB; 4KLE; X-ray; 1.97 A; A=1-335.
PDB; 4KLF; X-ray; 1.85 A; A=1-335.
PDB; 4KLG; X-ray; 1.70 A; A=1-335.
PDB; 4KLH; X-ray; 1.88 A; A=1-335.
PDB; 4KLI; X-ray; 1.60 A; A=1-335.
PDB; 4KLJ; X-ray; 1.80 A; A=1-335.
PDB; 4KLL; X-ray; 1.84 A; A=1-335.
PDB; 4KLM; X-ray; 1.75 A; A=1-335.
PDB; 4KLO; X-ray; 1.84 A; A=1-335.
PDB; 4KLQ; X-ray; 2.00 A; A=1-335.
PDB; 4KLS; X-ray; 1.98 A; A=1-335.
PDB; 4KLT; X-ray; 1.98 A; A=1-335.
PDB; 4KLU; X-ray; 1.97 A; A=1-335.
PDB; 4LVS; X-ray; 2.00 A; A=1-335.
PDB; 4M2Y; X-ray; 2.27 A; A=11-335.
PDB; 4M47; X-ray; 2.37 A; A=12-335.
PDB; 4M9G; X-ray; 2.01 A; A=1-335.
PDB; 4M9H; X-ray; 2.39 A; A=1-335.
PDB; 4M9J; X-ray; 2.04 A; A=1-335.
PDB; 4M9L; X-ray; 2.09 A; A=1-335.
PDB; 4M9N; X-ray; 2.28 A; A=1-335.
PDB; 4MF2; X-ray; 2.40 A; A=11-335.
PDB; 4MF8; X-ray; 2.32 A; A=7-335.
PDB; 4MFA; X-ray; 2.27 A; A=11-335.
PDB; 4MFC; X-ray; 2.13 A; A=11-335.
PDB; 4MFF; X-ray; 2.55 A; A=11-335.
PDB; 4NLK; X-ray; 2.49 A; A=7-335.
PDB; 4NLN; X-ray; 2.26 A; A=7-335.
PDB; 4NLZ; X-ray; 2.68 A; A=7-335.
PDB; 4NM1; X-ray; 2.42 A; A=7-335.
PDB; 4NM2; X-ray; 2.52 A; A=7-335.
PDB; 4NXZ; X-ray; 2.56 A; A=10-335.
PDB; 4NY8; X-ray; 2.25 A; A=10-335.
PDB; 4O5C; X-ray; 2.36 A; A=7-335.
PDB; 4O5E; X-ray; 2.53 A; A=7-335.
PDB; 4O5K; X-ray; 2.06 A; A=10-335.
PDB; 4O9M; X-ray; 2.30 A; A=1-335.
PDB; 4P2H; X-ray; 1.99 A; A=10-335.
PDB; 4PGQ; X-ray; 2.30 A; A=7-335.
PDB; 4PGX; X-ray; 2.08 A; A=10-335.
PDB; 4PGY; X-ray; 2.26 A; A=7-335.
PDB; 4PH5; X-ray; 2.55 A; A=10-335.
PDB; 4PHA; X-ray; 2.52 A; A=7-335.
PDB; 4PHD; X-ray; 2.21 A; A=7-335.
PDB; 4PHE; X-ray; 2.15 A; A=7-335.
PDB; 4PHP; X-ray; 2.60 A; A=10-335.
PDB; 4PPX; X-ray; 2.08 A; A=1-335.
PDB; 4R63; X-ray; 1.85 A; A=1-335.
PDB; 4R64; X-ray; 2.20 A; A=1-335.
PDB; 4R65; X-ray; 1.95 A; A=1-335.
PDB; 4R66; X-ray; 2.25 A; A=1-335.
PDB; 4RPX; X-ray; 1.90 A; A=1-335.
PDB; 4RPY; X-ray; 1.90 A; A=1-335.
PDB; 4RPZ; X-ray; 2.19 A; A=1-335.
PDB; 4RQ0; X-ray; 2.20 A; A=1-335.
PDB; 4RQ1; X-ray; 2.70 A; A=1-335.
PDB; 4RQ2; X-ray; 2.20 A; A=1-335.
PDB; 4RQ3; X-ray; 2.00 A; A=1-335.
PDB; 4RQ4; X-ray; 2.10 A; A=1-335.
PDB; 4RQ5; X-ray; 2.32 A; A=1-335.
PDB; 4RQ6; X-ray; 2.25 A; A=1-335.
PDB; 4RQ7; X-ray; 2.00 A; A=1-335.
PDB; 4RQ8; X-ray; 2.00 A; A=1-335.
PDB; 4RT2; X-ray; 1.92 A; A=1-335.
PDB; 4RT3; X-ray; 1.92 A; A=1-335.
PDB; 4TUP; X-ray; 1.80 A; A=7-335.
PDB; 4TUQ; X-ray; 2.37 A; A=10-335.
PDB; 4TUR; X-ray; 2.17 A; A=7-335.
PDB; 4TUS; X-ray; 2.42 A; A=10-335.
PDB; 4UAW; X-ray; 1.90 A; A=1-335.
PDB; 4UAY; X-ray; 1.98 A; A=1-335.
PDB; 4UAZ; X-ray; 1.88 A; A=1-335.
PDB; 4UB1; X-ray; 2.34 A; A=1-335.
PDB; 4UB2; X-ray; 2.51 A; A=1-335.
PDB; 4UB3; X-ray; 2.06 A; A=1-335.
PDB; 4UB4; X-ray; 1.95 A; A=1-335.
PDB; 4UB5; X-ray; 2.15 A; A=1-335.
PDB; 4UBB; X-ray; 1.90 A; A=1-335.
PDB; 4UBC; X-ray; 2.00 A; A=1-335.
PDB; 4YMM; X-ray; 2.20 A; A=1-335.
PDB; 4YMN; X-ray; 2.59 A; A=1-335.
PDB; 4YMO; X-ray; 2.15 A; A=1-335.
PDB; 4YN4; X-ray; 2.24 A; A=1-335.
PDB; 4Z6C; X-ray; 2.68 A; A=1-335.
PDB; 4Z6D; X-ray; 2.51 A; A=1-335.
PDB; 4Z6E; X-ray; 2.75 A; A=1-335.
PDB; 4Z6F; X-ray; 2.44 A; A=1-335.
PDB; 5BOL; X-ray; 1.98 A; A=1-335.
PDB; 5BOM; X-ray; 2.00 A; A=1-335.
PDB; 5BPC; X-ray; 2.00 A; A=1-335.
PDB; 5DB6; X-ray; 2.83 A; A=1-335.
PDB; 5DB7; X-ray; 2.21 A; A=1-335.
PDB; 5DB8; X-ray; 2.55 A; A=1-335.
PDB; 5DB9; X-ray; 2.45 A; A=1-335.
PDB; 5DBA; X-ray; 1.97 A; A=1-335.
PDB; 5DBB; X-ray; 2.25 A; A=1-335.
PDB; 5DBC; X-ray; 2.40 A; A=1-335.
PDB; 5EOZ; X-ray; 2.09 A; A=1-335.
PDB; 5HHH; X-ray; 2.36 A; A=9-335.
PDB; 5HHI; X-ray; 2.52 A; A=7-335.
PDB; 5J0O; X-ray; 2.00 A; A=1-335.
PDB; 5J0P; X-ray; 2.20 A; A=1-335.
PDB; 5J0Q; X-ray; 2.00 A; A=1-335.
PDB; 5J0R; X-ray; 2.00 A; A=1-335.
PDB; 5J0S; X-ray; 2.00 A; A=1-335.
PDB; 5J0T; X-ray; 2.00 A; A=1-335.
PDB; 5J0U; X-ray; 2.10 A; A=1-335.
PDB; 5J0W; X-ray; 2.40 A; A=1-335.
PDB; 5J0X; X-ray; 2.00 A; A=1-335.
PDB; 5J0Y; X-ray; 2.00 A; A=1-335.
PDB; 5J29; X-ray; 2.20 A; A=1-335.
PDB; 5J2A; X-ray; 2.50 A; A=1-335.
PDB; 5J2B; X-ray; 2.50 A; A=1-335.
PDB; 5J2C; X-ray; 2.10 A; A=1-335.
PDB; 5J2D; X-ray; 2.10 A; A=1-335.
PDB; 5J2E; X-ray; 2.10 A; A=1-335.
PDB; 5J2F; X-ray; 2.10 A; A=1-335.
PDB; 5J2G; X-ray; 2.10 A; A=1-335.
PDB; 5J2H; X-ray; 2.30 A; A=1-335.
PDB; 5J2I; X-ray; 2.40 A; A=1-335.
PDB; 5J2J; X-ray; 2.20 A; A=1-335.
PDB; 5J2K; X-ray; 2.10 A; A=1-335.
PDB; 5TB8; X-ray; 2.00 A; A=1-335.
PDB; 5TB9; X-ray; 2.49 A; A=1-335.
PDB; 5TBA; X-ray; 2.49 A; A=1-335.
PDB; 5TBB; X-ray; 2.39 A; A=1-335.
PDB; 5TBC; X-ray; 1.85 A; A=1-335.
PDB; 5TZV; X-ray; 2.00 A; A=1-335.
PDB; 5U2R; X-ray; 1.80 A; A=1-335.
PDB; 5U2S; X-ray; 2.30 A; A=1-335.
PDB; 5U2T; X-ray; 1.79 A; A=1-335.
PDB; 5U8G; X-ray; 2.17 A; A=1-335.
PDB; 5U8H; X-ray; 2.15 A; A=1-335.
PDB; 5U8I; X-ray; 2.45 A; A=1-335.
PDB; 5U9H; X-ray; 1.85 A; A=1-335.
PDB; 5UGN; X-ray; 2.00 A; A=1-335.
PDB; 5UGO; X-ray; 1.90 A; A=1-335.
PDB; 5UGP; X-ray; 1.96 A; A=1-335.
PDB; 5V1F; X-ray; 2.18 A; A=1-335.
PDB; 5V1G; X-ray; 1.80 A; A=1-335.
PDB; 5V1H; X-ray; 1.95 A; A=1-335.
PDB; 5V1I; X-ray; 2.04 A; A=1-335.
PDB; 5V1J; X-ray; 2.62 A; A=1-335.
PDB; 5V1N; X-ray; 2.00 A; A=1-335.
PDB; 5V1O; X-ray; 1.80 A; A=1-335.
PDB; 5V1P; X-ray; 1.99 A; A=1-335.
PDB; 5V1R; X-ray; 2.08 A; A=1-335.
PDB; 5VEZ; X-ray; 2.04 A; A=1-335.
PDB; 5VRW; X-ray; 2.58 A; A=1-335.
PDB; 5VRX; X-ray; 2.20 A; A=1-335.
PDB; 5VRY; X-ray; 1.90 A; A=1-335.
PDB; 5VRZ; X-ray; 2.05 A; A=1-335.
PDB; 5VS0; X-ray; 2.10 A; A=1-335.
PDB; 5VS1; X-ray; 2.50 A; A=1-335.
PDB; 5VS2; X-ray; 2.33 A; A=1-335.
PDB; 5VS3; X-ray; 1.70 A; A=1-335.
PDB; 5VS4; X-ray; 1.87 A; A=1-335.
PDB; 5WNX; X-ray; 2.55 A; A=1-335.
PDB; 5WNY; X-ray; 2.10 A; A=1-335.
PDB; 5WNZ; X-ray; 2.20 A; A=1-335.
PDB; 5WO0; X-ray; 1.60 A; A=1-335.
PDB; 6CR3; X-ray; 1.95 A; A=1-335.
PDB; 6CR4; X-ray; 1.80 A; A=1-335.
PDB; 6CR5; X-ray; 1.98 A; A=1-335.
PDB; 6CR6; X-ray; 2.10 A; A=1-335.
PDB; 6CR7; X-ray; 2.29 A; A=1-335.
PDB; 6CR8; X-ray; 2.05 A; A=1-335.
PDB; 6CR9; X-ray; 1.96 A; A=1-335.
PDB; 6CRB; X-ray; 2.15 A; A=1-335.
PDB; 6CRC; X-ray; 2.30 A; A=1-335.
PDB; 6CTI; X-ray; 2.00 A; A=1-335.
PDB; 6CTJ; X-ray; 2.10 A; A=1-335.
PDB; 6CTK; X-ray; 2.15 A; A=1-335.
PDB; 6CTL; X-ray; 2.00 A; A=1-335.
PDB; 6CTM; X-ray; 2.10 A; A=1-335.
PDB; 6CTN; X-ray; 1.92 A; A=1-335.
PDB; 6CTO; X-ray; 2.04 A; A=1-335.
PDB; 6CTP; X-ray; 2.20 A; A=1-335.
PDB; 6CTQ; X-ray; 1.87 A; A=1-335.
PDB; 6CTR; X-ray; 1.85 A; A=1-335.
PDB; 6CTT; X-ray; 2.00 A; A=1-335.
PDB; 6CTU; X-ray; 1.90 A; A=1-335.
PDB; 6CTV; X-ray; 2.02 A; A=1-335.
PDB; 6CTW; X-ray; 1.98 A; A=1-335.
PDB; 6CTX; X-ray; 2.02 A; A=1-335.
PDB; 6G2Q; X-ray; 2.15 A; A=1-335.
PDB; 7ICE; X-ray; 2.80 A; A=1-335.
PDB; 7ICF; X-ray; 3.10 A; A=1-335.
PDB; 7ICG; X-ray; 3.00 A; A=1-335.
PDB; 7ICH; X-ray; 2.90 A; A=1-335.
PDB; 7ICI; X-ray; 2.80 A; A=1-335.
PDB; 7ICJ; X-ray; 3.50 A; A=1-335.
PDB; 7ICK; X-ray; 2.90 A; A=1-335.
PDB; 7ICL; X-ray; 3.10 A; A=1-335.
PDB; 7ICM; X-ray; 3.00 A; A=1-335.
PDB; 7ICN; X-ray; 2.80 A; A=1-335.
PDB; 7ICO; X-ray; 3.30 A; A=1-335.
PDB; 7ICP; X-ray; 3.00 A; A=1-335.
PDB; 7ICQ; X-ray; 2.90 A; A=1-335.
PDB; 7ICR; X-ray; 3.00 A; A=1-335.
PDB; 7ICS; X-ray; 2.80 A; A=1-335.
PDB; 7ICT; X-ray; 2.80 A; A=1-335.
PDB; 7ICU; X-ray; 3.30 A; A=1-335.
PDB; 7ICV; X-ray; 2.80 A; A=1-335.
PDB; 8ICA; X-ray; 3.00 A; A=1-335.
PDB; 8ICB; X-ray; 3.10 A; A=1-335.
PDB; 8ICC; X-ray; 2.80 A; A=1-335.
PDB; 8ICE; X-ray; 3.20 A; A=1-335.
PDB; 8ICF; X-ray; 2.90 A; A=1-335.
PDB; 8ICG; X-ray; 3.30 A; A=1-335.
PDB; 8ICH; X-ray; 3.30 A; A=1-335.
PDB; 8ICI; X-ray; 2.80 A; A=1-335.
PDB; 8ICJ; X-ray; 3.20 A; A=1-335.
PDB; 8ICK; X-ray; 2.70 A; A=1-335.
PDB; 8ICL; X-ray; 3.10 A; A=1-335.
PDB; 8ICM; X-ray; 2.90 A; A=1-335.
PDB; 8ICN; X-ray; 2.80 A; A=1-335.
PDB; 8ICO; X-ray; 2.70 A; A=1-335.
PDB; 8ICP; X-ray; 2.90 A; A=1-335.
PDB; 8ICQ; X-ray; 3.00 A; A=1-335.
PDB; 8ICR; X-ray; 2.90 A; A=1-335.
PDB; 8ICS; X-ray; 2.90 A; A=1-335.
PDB; 8ICT; X-ray; 3.10 A; A=1-335.
PDB; 8ICU; X-ray; 3.00 A; A=1-335.
PDB; 8ICV; X-ray; 3.20 A; A=1-335.
PDB; 8ICW; X-ray; 3.30 A; A=1-335.
PDB; 8ICX; X-ray; 3.00 A; A=1-335.
PDB; 8ICY; X-ray; 3.10 A; A=1-335.
PDB; 8ICZ; X-ray; 3.10 A; A=1-335.
PDB; 9ICA; X-ray; 3.00 A; A=1-335.
PDB; 9ICB; X-ray; 3.20 A; A=1-335.
PDB; 9ICC; X-ray; 3.10 A; A=1-335.
PDB; 9ICE; X-ray; 3.30 A; A=1-335.
PDB; 9ICF; X-ray; 3.00 A; A=1-335.
PDB; 9ICG; X-ray; 3.00 A; A=1-335.
PDB; 9ICH; X-ray; 2.90 A; A=1-335.
PDB; 9ICI; X-ray; 3.10 A; A=1-335.
PDB; 9ICJ; X-ray; 3.10 A; A=1-335.
PDB; 9ICK; X-ray; 2.70 A; A=1-335.
PDB; 9ICL; X-ray; 2.80 A; A=1-335.
PDB; 9ICM; X-ray; 2.90 A; A=1-335.
PDB; 9ICN; X-ray; 3.00 A; A=1-335.
PDB; 9ICO; X-ray; 2.90 A; A=1-335.
PDB; 9ICP; X-ray; 3.10 A; A=1-335.
PDB; 9ICQ; X-ray; 2.90 A; A=1-335.
PDB; 9ICR; X-ray; 3.00 A; A=1-335.
PDB; 9ICS; X-ray; 2.90 A; A=1-335.
PDB; 9ICT; X-ray; 3.00 A; A=1-335.
PDB; 9ICU; X-ray; 2.90 A; A=1-335.
PDB; 9ICV; X-ray; 2.70 A; A=1-335.
PDB; 9ICW; X-ray; 2.60 A; A=1-335.
PDB; 9ICX; X-ray; 2.60 A; A=1-335.
PDB; 9ICY; X-ray; 3.00 A; A=1-335.
PDBsum; 1BPX; -.
PDBsum; 1BPY; -.
PDBsum; 1BPZ; -.
PDBsum; 1MQ2; -.
PDBsum; 1MQ3; -.
PDBsum; 1TV9; -.
PDBsum; 1TVA; -.
PDBsum; 1ZJM; -.
PDBsum; 1ZJN; -.
PDBsum; 1ZQA; -.
PDBsum; 1ZQB; -.
PDBsum; 1ZQC; -.
PDBsum; 1ZQD; -.
PDBsum; 1ZQE; -.
PDBsum; 1ZQF; -.
PDBsum; 1ZQG; -.
PDBsum; 1ZQH; -.
PDBsum; 1ZQI; -.
PDBsum; 1ZQJ; -.
PDBsum; 1ZQK; -.
PDBsum; 1ZQL; -.
PDBsum; 1ZQM; -.
PDBsum; 1ZQN; -.
PDBsum; 1ZQO; -.
PDBsum; 1ZQP; -.
PDBsum; 1ZQQ; -.
PDBsum; 1ZQR; -.
PDBsum; 1ZQS; -.
PDBsum; 1ZQT; -.
PDBsum; 2FMP; -.
PDBsum; 2FMQ; -.
PDBsum; 2FMS; -.
PDBsum; 2I9G; -.
PDBsum; 2ISO; -.
PDBsum; 2ISP; -.
PDBsum; 2P66; -.
PDBsum; 2PXI; -.
PDBsum; 3C2K; -.
PDBsum; 3C2L; -.
PDBsum; 3C2M; -.
PDBsum; 3GDX; -.
PDBsum; 3ISB; -.
PDBsum; 3ISC; -.
PDBsum; 3ISD; -.
PDBsum; 3JPN; -.
PDBsum; 3JPO; -.
PDBsum; 3JPP; -.
PDBsum; 3JPQ; -.
PDBsum; 3JPR; -.
PDBsum; 3JPS; -.
PDBsum; 3JPT; -.
PDBsum; 3LK9; -.
PDBsum; 3MBY; -.
PDBsum; 3OGU; -.
PDBsum; 3RH4; -.
PDBsum; 3RH5; -.
PDBsum; 3RH6; -.
PDBsum; 3RJE; -.
PDBsum; 3RJF; -.
PDBsum; 3RJG; -.
PDBsum; 3RJH; -.
PDBsum; 3RJI; -.
PDBsum; 3RJJ; -.
PDBsum; 3RJK; -.
PDBsum; 3TFR; -.
PDBsum; 3TFS; -.
PDBsum; 4DO9; -.
PDBsum; 4DOA; -.
PDBsum; 4DOB; -.
PDBsum; 4DOC; -.
PDBsum; 4F5N; -.
PDBsum; 4F5O; -.
PDBsum; 4F5P; -.
PDBsum; 4F5Q; -.
PDBsum; 4F5R; -.
PDBsum; 4GXI; -.
PDBsum; 4GXJ; -.
PDBsum; 4GXK; -.
PDBsum; 4JWM; -.
PDBsum; 4JWN; -.
PDBsum; 4KLD; -.
PDBsum; 4KLE; -.
PDBsum; 4KLF; -.
PDBsum; 4KLG; -.
PDBsum; 4KLH; -.
PDBsum; 4KLI; -.
PDBsum; 4KLJ; -.
PDBsum; 4KLL; -.
PDBsum; 4KLM; -.
PDBsum; 4KLO; -.
PDBsum; 4KLQ; -.
PDBsum; 4KLS; -.
PDBsum; 4KLT; -.
PDBsum; 4KLU; -.
PDBsum; 4LVS; -.
PDBsum; 4M2Y; -.
PDBsum; 4M47; -.
PDBsum; 4M9G; -.
PDBsum; 4M9H; -.
PDBsum; 4M9J; -.
PDBsum; 4M9L; -.
PDBsum; 4M9N; -.
PDBsum; 4MF2; -.
PDBsum; 4MF8; -.
PDBsum; 4MFA; -.
PDBsum; 4MFC; -.
PDBsum; 4MFF; -.
PDBsum; 4NLK; -.
PDBsum; 4NLN; -.
PDBsum; 4NLZ; -.
PDBsum; 4NM1; -.
PDBsum; 4NM2; -.
PDBsum; 4NXZ; -.
PDBsum; 4NY8; -.
PDBsum; 4O5C; -.
PDBsum; 4O5E; -.
PDBsum; 4O5K; -.
PDBsum; 4O9M; -.
PDBsum; 4P2H; -.
PDBsum; 4PGQ; -.
PDBsum; 4PGX; -.
PDBsum; 4PGY; -.
PDBsum; 4PH5; -.
PDBsum; 4PHA; -.
PDBsum; 4PHD; -.
PDBsum; 4PHE; -.
PDBsum; 4PHP; -.
PDBsum; 4PPX; -.
PDBsum; 4R63; -.
PDBsum; 4R64; -.
PDBsum; 4R65; -.
PDBsum; 4R66; -.
PDBsum; 4RPX; -.
PDBsum; 4RPY; -.
PDBsum; 4RPZ; -.
PDBsum; 4RQ0; -.
PDBsum; 4RQ1; -.
PDBsum; 4RQ2; -.
PDBsum; 4RQ3; -.
PDBsum; 4RQ4; -.
PDBsum; 4RQ5; -.
PDBsum; 4RQ6; -.
PDBsum; 4RQ7; -.
PDBsum; 4RQ8; -.
PDBsum; 4RT2; -.
PDBsum; 4RT3; -.
PDBsum; 4TUP; -.
PDBsum; 4TUQ; -.
PDBsum; 4TUR; -.
PDBsum; 4TUS; -.
PDBsum; 4UAW; -.
PDBsum; 4UAY; -.
PDBsum; 4UAZ; -.
PDBsum; 4UB1; -.
PDBsum; 4UB2; -.
PDBsum; 4UB3; -.
PDBsum; 4UB4; -.
PDBsum; 4UB5; -.
PDBsum; 4UBB; -.
PDBsum; 4UBC; -.
PDBsum; 4YMM; -.
PDBsum; 4YMN; -.
PDBsum; 4YMO; -.
PDBsum; 4YN4; -.
PDBsum; 4Z6C; -.
PDBsum; 4Z6D; -.
PDBsum; 4Z6E; -.
PDBsum; 4Z6F; -.
PDBsum; 5BOL; -.
PDBsum; 5BOM; -.
PDBsum; 5BPC; -.
PDBsum; 5DB6; -.
PDBsum; 5DB7; -.
PDBsum; 5DB8; -.
PDBsum; 5DB9; -.
PDBsum; 5DBA; -.
PDBsum; 5DBB; -.
PDBsum; 5DBC; -.
PDBsum; 5EOZ; -.
PDBsum; 5HHH; -.
PDBsum; 5HHI; -.
PDBsum; 5J0O; -.
PDBsum; 5J0P; -.
PDBsum; 5J0Q; -.
PDBsum; 5J0R; -.
PDBsum; 5J0S; -.
PDBsum; 5J0T; -.
PDBsum; 5J0U; -.
PDBsum; 5J0W; -.
PDBsum; 5J0X; -.
PDBsum; 5J0Y; -.
PDBsum; 5J29; -.
PDBsum; 5J2A; -.
PDBsum; 5J2B; -.
PDBsum; 5J2C; -.
PDBsum; 5J2D; -.
PDBsum; 5J2E; -.
PDBsum; 5J2F; -.
PDBsum; 5J2G; -.
PDBsum; 5J2H; -.
PDBsum; 5J2I; -.
PDBsum; 5J2J; -.
PDBsum; 5J2K; -.
PDBsum; 5TB8; -.
PDBsum; 5TB9; -.
PDBsum; 5TBA; -.
PDBsum; 5TBB; -.
PDBsum; 5TBC; -.
PDBsum; 5TZV; -.
PDBsum; 5U2R; -.
PDBsum; 5U2S; -.
PDBsum; 5U2T; -.
PDBsum; 5U8G; -.
PDBsum; 5U8H; -.
PDBsum; 5U8I; -.
PDBsum; 5U9H; -.
PDBsum; 5UGN; -.
PDBsum; 5UGO; -.
PDBsum; 5UGP; -.
PDBsum; 5V1F; -.
PDBsum; 5V1G; -.
PDBsum; 5V1H; -.
PDBsum; 5V1I; -.
PDBsum; 5V1J; -.
PDBsum; 5V1N; -.
PDBsum; 5V1O; -.
PDBsum; 5V1P; -.
PDBsum; 5V1R; -.
PDBsum; 5VEZ; -.
PDBsum; 5VRW; -.
PDBsum; 5VRX; -.
PDBsum; 5VRY; -.
PDBsum; 5VRZ; -.
PDBsum; 5VS0; -.
PDBsum; 5VS1; -.
PDBsum; 5VS2; -.
PDBsum; 5VS3; -.
PDBsum; 5VS4; -.
PDBsum; 5WNX; -.
PDBsum; 5WNY; -.
PDBsum; 5WNZ; -.
PDBsum; 5WO0; -.
PDBsum; 6CR3; -.
PDBsum; 6CR4; -.
PDBsum; 6CR5; -.
PDBsum; 6CR6; -.
PDBsum; 6CR7; -.
PDBsum; 6CR8; -.
PDBsum; 6CR9; -.
PDBsum; 6CRB; -.
PDBsum; 6CRC; -.
PDBsum; 6CTI; -.
PDBsum; 6CTJ; -.
PDBsum; 6CTK; -.
PDBsum; 6CTL; -.
PDBsum; 6CTM; -.
PDBsum; 6CTN; -.
PDBsum; 6CTO; -.
PDBsum; 6CTP; -.
PDBsum; 6CTQ; -.
PDBsum; 6CTR; -.
PDBsum; 6CTT; -.
PDBsum; 6CTU; -.
PDBsum; 6CTV; -.
PDBsum; 6CTW; -.
PDBsum; 6CTX; -.
PDBsum; 6G2Q; -.
PDBsum; 7ICE; -.
PDBsum; 7ICF; -.
PDBsum; 7ICG; -.
PDBsum; 7ICH; -.
PDBsum; 7ICI; -.
PDBsum; 7ICJ; -.
PDBsum; 7ICK; -.
PDBsum; 7ICL; -.
PDBsum; 7ICM; -.
PDBsum; 7ICN; -.
PDBsum; 7ICO; -.
PDBsum; 7ICP; -.
PDBsum; 7ICQ; -.
PDBsum; 7ICR; -.
PDBsum; 7ICS; -.
PDBsum; 7ICT; -.
PDBsum; 7ICU; -.
PDBsum; 7ICV; -.
PDBsum; 8ICA; -.
PDBsum; 8ICB; -.
PDBsum; 8ICC; -.
PDBsum; 8ICE; -.
PDBsum; 8ICF; -.
PDBsum; 8ICG; -.
PDBsum; 8ICH; -.
PDBsum; 8ICI; -.
PDBsum; 8ICJ; -.
PDBsum; 8ICK; -.
PDBsum; 8ICL; -.
PDBsum; 8ICM; -.
PDBsum; 8ICN; -.
PDBsum; 8ICO; -.
PDBsum; 8ICP; -.
PDBsum; 8ICQ; -.
PDBsum; 8ICR; -.
PDBsum; 8ICS; -.
PDBsum; 8ICT; -.
PDBsum; 8ICU; -.
PDBsum; 8ICV; -.
PDBsum; 8ICW; -.
PDBsum; 8ICX; -.
PDBsum; 8ICY; -.
PDBsum; 8ICZ; -.
PDBsum; 9ICA; -.
PDBsum; 9ICB; -.
PDBsum; 9ICC; -.
PDBsum; 9ICE; -.
PDBsum; 9ICF; -.
PDBsum; 9ICG; -.
PDBsum; 9ICH; -.
PDBsum; 9ICI; -.
PDBsum; 9ICJ; -.
PDBsum; 9ICK; -.
PDBsum; 9ICL; -.
PDBsum; 9ICM; -.
PDBsum; 9ICN; -.
PDBsum; 9ICO; -.
PDBsum; 9ICP; -.
PDBsum; 9ICQ; -.
PDBsum; 9ICR; -.
PDBsum; 9ICS; -.
PDBsum; 9ICT; -.
PDBsum; 9ICU; -.
PDBsum; 9ICV; -.
PDBsum; 9ICW; -.
PDBsum; 9ICX; -.
PDBsum; 9ICY; -.
ProteinModelPortal; P06746; -.
SMR; P06746; -.
BioGrid; 111419; 39.
CORUM; P06746; -.
IntAct; P06746; 17.
STRING; 9606.ENSP00000265421; -.
BindingDB; P06746; -.
ChEMBL; CHEMBL2392; -.
DrugBank; DB03222; 2'-Deoxyadenosine 5'-Triphosphate.
DrugBank; DB00987; Cytarabine.
iPTMnet; P06746; -.
PhosphoSitePlus; P06746; -.
BioMuta; POLB; -.
DMDM; 544186; -.
EPD; P06746; -.
MaxQB; P06746; -.
PaxDb; P06746; -.
PeptideAtlas; P06746; -.
PRIDE; P06746; -.
ProteomicsDB; 51926; -.
DNASU; 5423; -.
Ensembl; ENST00000265421; ENSP00000265421; ENSG00000070501.
GeneID; 5423; -.
KEGG; hsa:5423; -.
UCSC; uc003xoz.3; human.
CTD; 5423; -.
DisGeNET; 5423; -.
EuPathDB; HostDB:ENSG00000070501.11; -.
GeneCards; POLB; -.
HGNC; HGNC:9174; POLB.
HPA; CAB011616; -.
HPA; HPA049104; -.
MIM; 174760; gene.
neXtProt; NX_P06746; -.
OpenTargets; ENSG00000070501; -.
PharmGKB; PA276; -.
eggNOG; KOG2534; Eukaryota.
eggNOG; COG1796; LUCA.
GeneTree; ENSGT00530000063002; -.
HOGENOM; HOG000007787; -.
HOVERGEN; HBG002359; -.
InParanoid; P06746; -.
KO; K02330; -.
OMA; DLFNKNM; -.
OrthoDB; EOG091G0HMG; -.
PhylomeDB; P06746; -.
TreeFam; TF103002; -.
BRENDA; 2.7.7.7; 2681.
BRENDA; 4.2.99.B1; 2681.
Reactome; R-HSA-110362; POLB-Dependent Long Patch Base Excision Repair.
Reactome; R-HSA-110373; Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
Reactome; R-HSA-110381; Resolution of AP sites via the single-nucleotide replacement pathway.
Reactome; R-HSA-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-73930; Abasic sugar-phosphate removal via the single-nucleotide replacement pathway.
SIGNOR; P06746; -.
ChiTaRS; POLB; human.
EvolutionaryTrace; P06746; -.
GeneWiki; DNA_polymerase_beta; -.
GenomeRNAi; 5423; -.
PRO; PR:P06746; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000070501; Expressed in 225 organ(s), highest expression level in cerebellar hemisphere.
CleanEx; HS_POLB; -.
ExpressionAtlas; P06746; baseline and differential.
Genevisible; P06746; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0005876; C:spindle microtubule; IDA:MGI.
GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; TAS:Reactome.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IDA:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
GO; GO:0006286; P:base-excision repair, base-free sugar-phosphate removal; TAS:Reactome.
GO; GO:0006288; P:base-excision repair, DNA ligation; TAS:Reactome.
GO; GO:0006287; P:base-excision repair, gap-filling; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0006261; P:DNA-dependent DNA replication; TAS:ProtInc.
GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
GO; GO:0071707; P:immunoglobulin heavy chain V-D-J recombination; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0048535; P:lymph node development; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006290; P:pyrimidine dimer repair; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0007435; P:salivary gland morphogenesis; IEA:Ensembl.
GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IEA:Ensembl.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
CDD; cd00141; NT_POLXc; 1.
Gene3D; 1.10.150.110; -; 1.
Gene3D; 3.30.210.10; -; 1.
InterPro; IPR002054; DNA-dir_DNA_pol_X.
InterPro; IPR019843; DNA_pol-X_BS.
InterPro; IPR010996; DNA_pol_b-like_N.
InterPro; IPR028207; DNA_pol_B_palm_palm.
InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
InterPro; IPR037160; DNA_Pol_thumb_sf.
InterPro; IPR022312; DNA_pol_X.
InterPro; IPR002008; DNA_pol_X_beta-like.
InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
InterPro; IPR029398; PolB_thumb.
Pfam; PF14792; DNA_pol_B_palm; 1.
Pfam; PF14791; DNA_pol_B_thumb; 1.
Pfam; PF10391; DNA_pol_lambd_f; 1.
Pfam; PF14716; HHH_8; 1.
PRINTS; PR00869; DNAPOLX.
PRINTS; PR00870; DNAPOLXBETA.
SMART; SM00278; HhH1; 2.
SMART; SM00483; POLXc; 1.
SUPFAM; SSF47802; SSF47802; 1.
PROSITE; PS00522; DNA_POLYMERASE_X; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm; DNA damage;
DNA repair; DNA replication; DNA synthesis; DNA-binding;
DNA-directed DNA polymerase; Isopeptide bond; Lyase; Magnesium;
Metal-binding; Methylation; Nucleotidyltransferase; Nucleus;
Polymorphism; Reference proteome; Sodium; Transferase;
Ubl conjugation.
CHAIN 1 335 DNA polymerase beta.
/FTId=PRO_0000218778.
REGION 183 192 DNA binding.
ACT_SITE 72 72 Schiff-base intermediate with DNA.
METAL 101 101 Sodium; via carbonyl oxygen.
METAL 103 103 Sodium; via carbonyl oxygen.
METAL 106 106 Sodium; via carbonyl oxygen.
METAL 190 190 Magnesium 1.
METAL 190 190 Magnesium 2.
METAL 192 192 Magnesium 1.
METAL 192 192 Magnesium 2.
METAL 256 256 Magnesium 2.
MOD_RES 72 72 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K409}.
MOD_RES 83 83 Omega-N-methylarginine; by PRMT6.
{ECO:0000269|PubMed:16600869}.
MOD_RES 152 152 Omega-N-methylarginine; by PRMT6.
{ECO:0000269|PubMed:16600869}.
CROSSLNK 41 41 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19713937,
ECO:0000269|PubMed:21362556}.
CROSSLNK 61 61 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19713937,
ECO:0000269|PubMed:21362556}.
CROSSLNK 81 81 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:19713937,
ECO:0000269|PubMed:21362556}.
VARIANT 242 242 P -> R (in dbSNP:rs3136797).
{ECO:0000269|Ref.6}.
/FTId=VAR_018881.
MUTAGEN 35 35 K->Q,R: Reduces DNA lyase activity
slightly. {ECO:0000269|PubMed:9572863}.
MUTAGEN 39 39 Y->Q: Abolishes DNA polymerase and DNA
lyase activity.
{ECO:0000269|PubMed:9572863}.
MUTAGEN 41 41 K->R: Abolishes ubiquitination; when
associated with R-61 and R-81.
{ECO:0000269|PubMed:19713937}.
MUTAGEN 61 61 K->R: Abolishes ubiquitination; when
associated with R-41 and R-81.
{ECO:0000269|PubMed:19713937}.
MUTAGEN 68 68 K->Q,R: Reduces DNA lyase activity
slightly. {ECO:0000269|PubMed:9572863}.
MUTAGEN 72 72 K->Q,R: Abolishes DNA lyase activity. No
effect on DNA polymerase activity.
{ECO:0000269|PubMed:9572863}.
MUTAGEN 81 81 K->R: Abolishes ubiquitination; when
associated with R-41 and R-61.
{ECO:0000269|PubMed:19713937}.
MUTAGEN 83 83 R->K: Slight effect. Abolishes
methylation by PRMT6 and impairs the
polymerase activity; when associated with
K-152. {ECO:0000269|PubMed:16600869}.
MUTAGEN 84 84 K->R: No effect.
{ECO:0000269|PubMed:9572863}.
MUTAGEN 152 152 R->K: Slight effect. Abolishes
methylation by PRMT6 and impairs the
polymerase activity; when associated with
K-83. {ECO:0000269|PubMed:16600869}.
CONFLICT 18 18 M -> K (in Ref. 3; AAB60688).
{ECO:0000305}.
CONFLICT 228 228 L -> R (in Ref. 10; AAA60133).
{ECO:0000305}.
CONFLICT 260 260 I -> Y (in Ref. 10; AAA60133).
{ECO:0000305}.
CONFLICT 287 287 L -> K (in Ref. 10; AAA60133).
{ECO:0000305}.
TURN 9 12 {ECO:0000244|PDB:5U2T}.
HELIX 13 28 {ECO:0000244|PDB:4KLI}.
HELIX 33 48 {ECO:0000244|PDB:4KLI}.
HELIX 56 60 {ECO:0000244|PDB:4KLI}.
STRAND 62 64 {ECO:0000244|PDB:1BPY}.
HELIX 67 79 {ECO:0000244|PDB:4KLI}.
HELIX 83 90 {ECO:0000244|PDB:4KLI}.
HELIX 92 100 {ECO:0000244|PDB:4KLI}.
TURN 101 105 {ECO:0000244|PDB:1ZQD}.
HELIX 108 116 {ECO:0000244|PDB:4KLI}.
HELIX 122 127 {ECO:0000244|PDB:4KLI}.
HELIX 128 131 {ECO:0000244|PDB:4KLI}.
HELIX 134 141 {ECO:0000244|PDB:4KLI}.
HELIX 143 146 {ECO:0000244|PDB:4KLI}.
HELIX 152 169 {ECO:0000244|PDB:4KLI}.
STRAND 174 177 {ECO:0000244|PDB:4KLI}.
HELIX 179 182 {ECO:0000244|PDB:4KLI}.
STRAND 186 196 {ECO:0000244|PDB:4KLI}.
STRAND 202 204 {ECO:0000244|PDB:3OGU}.
STRAND 207 209 {ECO:0000244|PDB:4KLL}.
HELIX 210 220 {ECO:0000244|PDB:4KLI}.
STRAND 224 230 {ECO:0000244|PDB:4KLI}.
STRAND 232 239 {ECO:0000244|PDB:4KLI}.
STRAND 245 247 {ECO:0000244|PDB:4R63}.
STRAND 253 259 {ECO:0000244|PDB:4KLI}.
HELIX 262 264 {ECO:0000244|PDB:4KLI}.
HELIX 265 273 {ECO:0000244|PDB:4KLI}.
HELIX 276 289 {ECO:0000244|PDB:4KLI}.
STRAND 291 293 {ECO:0000244|PDB:4KLI}.
STRAND 298 301 {ECO:0000244|PDB:4KLI}.
STRAND 303 305 {ECO:0000244|PDB:4KLI}.
HELIX 316 322 {ECO:0000244|PDB:4KLI}.
HELIX 330 332 {ECO:0000244|PDB:4KLI}.
SEQUENCE 335 AA; 38178 MW; FF9A6D0E6F9A9487 CRC64;
MSKRKAPQET LNGGITDMLT ELANFEKNVS QAIHKYNAYR KAASVIAKYP HKIKSGAEAK
KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL TRVSGIGPSA ARKFVDEGIK
TLEDLRKNED KLNHHQRIGL KYFGDFEKRI PREEMLQMQD IVLNEVKKVD SEYIATVCGS
FRRGAESSGD MDVLLTHPSF TSESTKQPKL LHQVVEQLQK VHFITDTLSK GETKFMGVCQ
LPSKNDEKEY PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP
LGVTGVAGEP LPVDSEKDIF DYIQWKYREP KDRSE


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