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Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase (XD) (EC 1.17.1.4); Xanthine oxidase (XO) (EC 1.17.3.2) (Xanthine oxidoreductase) (XOR)]

 XDH_BOVIN               Reviewed;        1332 AA.
P80457; Q95325;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
22-NOV-2017, entry version 154.
RecName: Full=Xanthine dehydrogenase/oxidase;
Includes:
RecName: Full=Xanthine dehydrogenase;
Short=XD;
EC=1.17.1.4 {ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:4352904};
Includes:
RecName: Full=Xanthine oxidase;
Short=XO;
EC=1.17.3.2 {ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:4352904};
AltName: Full=Xanthine oxidoreductase;
Short=XOR;
Name=XDH;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=8708081; DOI=10.3168/jds.S0022-0302(96)76351-8;
Berglund L., Rasmussen J.T., Andersen M.D., Rasmussen M.S.,
Petersen T.E.;
"Purification of the bovine xanthine oxidoreductase from milk fat
globule membranes and cloning of complementary deoxyribonucleic
acid.";
J. Dairy Sci. 79:198-204(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=9388547; DOI=10.1042/bst0250791;
Terao M., Kurosaki M., Zanotta S., Garattini E.;
"The xanthine oxidoreductase gene: structure and regulation.";
Biochem. Soc. Trans. 25:791-796(1997).
[3]
PROTEIN SEQUENCE OF 2-23; 186-205 AND 552-562.
TISSUE=Milk;
PubMed=7556219; DOI=10.1111/j.1432-1033.1995.646zz.x;
Turner N.A., Doyle W.A., Ventom A.M., Bray R.C.;
"Properties of rabbit liver aldehyde oxidase and the relationship of
the enzyme to xanthine oxidase and dehydrogenase.";
Eur. J. Biochem. 232:646-657(1995).
[4]
CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
AND CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS.
PubMed=4352904; DOI=10.1042/bj1310191;
Battelli M.G., Lorenzoni E., Stripe F.;
"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase).
Purification, interconversion and some properties.";
Biochem. J. 131:191-198(1973).
[5]
ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
ARG-335; TRP-336 AND ARG-427.
PubMed=12817083; DOI=10.1073/pnas.1431485100;
Kuwabara Y., Nishino T., Okamoto K., Matsumura T., Eger B.T.,
Pai E.F., Nishino T.;
"Unique amino acids cluster for switching from the dehydrogenase to
oxidase form of xanthine oxidoreductase.";
Proc. Natl. Acad. Sci. U.S.A. 100:8170-8175(2003).
[6]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD;
IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC
ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=11005854; DOI=10.1073/pnas.97.20.10723;
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.;
"Crystal structures of bovine milk xanthine dehydrogenase and xanthine
oxidase: structure-based mechanism of conversion.";
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000).
[7]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD;
MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720,
COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=12421831; DOI=10.1074/jbc.M208307200;
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.;
"An extremely potent inhibitor of xanthine oxidoreductase. Crystal
structure of the enzyme-inhibitor complex and mechanism of
inhibition.";
J. Biol. Chem. 278:1848-1855(2003).
[8]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD;
MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE,
COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=15148401; DOI=10.1073/pnas.0400973101;
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.;
"The crystal structure of xanthine oxidoreductase during catalysis:
implications for reaction mechanism and enzyme inhibition.";
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004).
[9]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH FAD;
MOLYBDOPTERIN; IRON-SULFUR CENTERS; CALCIUM IONS; XANTHINE AND
LUMAZINE, COFACTOR, AND SUBUNIT.
PubMed=19109252; DOI=10.1074/jbc.M804517200;
Pauff J.M., Cao H., Hille R.;
"Substrate orientation and catalysis at the molybdenum site in
xanthine oxidase: crystal structures in complex with xanthine and
lumazine.";
J. Biol. Chem. 284:8760-8767(2009).
-!- FUNCTION: Key enzyme in purine degradation. Catalyzes the
oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of
xanthine to uric acid. Contributes to the generation of reactive
oxygen species. {ECO:0000250|UniProtKB:P22985}.
-!- CATALYTIC ACTIVITY: Xanthine + NAD(+) + H(2)O = urate + NADH.
{ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831,
ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:4352904}.
-!- CATALYTIC ACTIVITY: Hypoxanthine + NAD(+) + H(2)O = xanthine +
NADH. {ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831,
ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:4352904}.
-!- CATALYTIC ACTIVITY: Xanthine + H(2)O + O(2) = urate + H(2)O(2).
{ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831,
ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:4352904}.
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Note=Binds 2 [2Fe-2S] clusters.;
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
-!- COFACTOR:
Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.;
-!- ENZYME REGULATION: Can be converted from the dehydrogenase form
(D) to the oxidase form (O) irreversibly by proteolysis or
reversibly through the oxidation of sulfhydryl groups.
{ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12817083,
ECO:0000269|PubMed:4352904}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=111 uM for molecular oxygen in dehydrogenase form
{ECO:0000269|PubMed:12817083, ECO:0000269|PubMed:4352904};
KM=37.7 uM for molecular oxygen in oxygenase form
{ECO:0000269|PubMed:12817083, ECO:0000269|PubMed:4352904};
KM=20.8 uM for NAD {ECO:0000269|PubMed:12817083,
ECO:0000269|PubMed:4352904};
KM=5 uM for xanthine {ECO:0000269|PubMed:12817083,
ECO:0000269|PubMed:4352904};
-!- SUBUNIT: Homodimer. Interacts with BTN1A1 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Peroxisome.
Secreted.
-!- TISSUE SPECIFICITY: Detected in milk (at protein level).
{ECO:0000269|PubMed:11005854, ECO:0000269|PubMed:12421831,
ECO:0000269|PubMed:15148401}.
-!- PTM: Subject to partial proteolysis; this alters the enzyme from
the dehydrogenase form (D) to the oxidase form (O).
-!- PTM: Contains sulfhydryl groups that are easily oxidized (in
vitro); this alters the enzyme from the dehydrogenase form (D) to
the oxidase form (O).
-!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/XO/";
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EMBL; X83508; CAA58497.1; -; mRNA.
EMBL; X98491; CAA67117.1; -; mRNA.
PIR; S65135; S65135.
RefSeq; NP_776397.1; NM_173972.2.
UniGene; Bt.5403; -.
PDB; 1FIQ; X-ray; 2.50 A; A=1-219, B=220-569, C=570-1332.
PDB; 1FO4; X-ray; 2.10 A; A/B=1-1332.
PDB; 1N5X; X-ray; 2.80 A; A/B=2-1332.
PDB; 1V97; X-ray; 1.94 A; A/B=1-1332.
PDB; 1VDV; X-ray; 1.98 A; A/B=1-1332.
PDB; 3AM9; X-ray; 2.17 A; A/B=1-1332.
PDB; 3AMZ; X-ray; 2.10 A; A/B=1-1332.
PDB; 3AX7; X-ray; 2.34 A; A/B=1-1332.
PDB; 3AX9; X-ray; 2.30 A; A/B=1-1332.
PDB; 3B9J; X-ray; 2.30 A; A/I=1-219, B/J=220-569, C/K=570-1332.
PDB; 3BDJ; X-ray; 2.00 A; A/B=1-1332.
PDB; 3ETR; X-ray; 2.20 A; A/L=2-165, B/M=224-528, C/N=571-1325.
PDB; 3EUB; X-ray; 2.60 A; 2/A/J/S=1-165, 3/B/K/T=224-528, 4/C/L/U=571-1332.
PDB; 3NRZ; X-ray; 1.80 A; A/J=2-165, B/K=224-528, C/L=571-1326.
PDB; 3NS1; X-ray; 2.60 A; A/J=2-165, B/K=224-528, C/L=571-1325.
PDB; 3NVV; X-ray; 1.82 A; A/J=2-165, B/K=195-528, C/L=571-1325.
PDB; 3NVW; X-ray; 1.60 A; A/J=2-165, B/K=195-528, C/L=571-1326.
PDB; 3NVY; X-ray; 2.00 A; A/J=2-165, B/K=195-528, C/L=571-1326.
PDB; 3NVZ; X-ray; 1.60 A; A/J=2-165, B/K=224-528, C/L=571-1325.
PDB; 3SR6; X-ray; 2.10 A; A/J=2-165, B/K=224-528, C/L=571-1315.
PDB; 3UNA; X-ray; 1.90 A; A/B=1-1332.
PDB; 3UNC; X-ray; 1.65 A; A/B=1-1332.
PDB; 3UNI; X-ray; 2.20 A; A/B=1-1332.
PDBsum; 1FIQ; -.
PDBsum; 1FO4; -.
PDBsum; 1N5X; -.
PDBsum; 1V97; -.
PDBsum; 1VDV; -.
PDBsum; 3AM9; -.
PDBsum; 3AMZ; -.
PDBsum; 3AX7; -.
PDBsum; 3AX9; -.
PDBsum; 3B9J; -.
PDBsum; 3BDJ; -.
PDBsum; 3ETR; -.
PDBsum; 3EUB; -.
PDBsum; 3NRZ; -.
PDBsum; 3NS1; -.
PDBsum; 3NVV; -.
PDBsum; 3NVW; -.
PDBsum; 3NVY; -.
PDBsum; 3NVZ; -.
PDBsum; 3SR6; -.
PDBsum; 3UNA; -.
PDBsum; 3UNC; -.
PDBsum; 3UNI; -.
DisProt; DP00450; -.
ProteinModelPortal; P80457; -.
SMR; P80457; -.
STRING; 9913.ENSBTAP00000016620; -.
BindingDB; P80457; -.
ChEMBL; CHEMBL3649; -.
PaxDb; P80457; -.
PeptideAtlas; P80457; -.
PRIDE; P80457; -.
GeneID; 280960; -.
KEGG; bta:280960; -.
CTD; 7498; -.
eggNOG; KOG0430; Eukaryota.
eggNOG; COG4630; LUCA.
eggNOG; COG4631; LUCA.
HOGENOM; HOG000191197; -.
HOVERGEN; HBG004182; -.
InParanoid; P80457; -.
KO; K00106; -.
BRENDA; 1.17.1.4; 908.
BRENDA; 1.17.3.2; 908.
SABIO-RK; P80457; -.
EvolutionaryTrace; P80457; -.
PRO; PR:P80457; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; IDA:CAFA.
GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
GO; GO:0002197; C:xanthine dehydrogenase complex; IDA:CAFA.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:CAFA.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0071949; F:FAD binding; IDA:CAFA.
GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0030151; F:molybdenum ion binding; IDA:CAFA.
GO; GO:0043546; F:molybdopterin cofactor binding; IDA:CAFA.
GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0004854; F:xanthine dehydrogenase activity; ISS:UniProtKB.
GO; GO:0004855; F:xanthine oxidase activity; ISS:UniProtKB.
GO; GO:0009115; P:xanthine catabolic process; ISS:UniProtKB.
Gene3D; 1.10.150.120; -; 1.
Gene3D; 3.10.20.30; -; 1.
Gene3D; 3.30.365.10; -; 4.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.30.465.10; -; 1.
Gene3D; 3.90.1170.50; -; 1.
InterPro; IPR002888; 2Fe-2S-bd.
InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR006058; 2Fe2S_fd_BS.
InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
InterPro; IPR016208; Ald_Oxase/xanthine_DH.
InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
InterPro; IPR012675; Beta-grasp_dom_sf.
InterPro; IPR005107; CO_DH_flav_C.
InterPro; IPR036683; CO_DH_flav_C_dom_sf.
InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
InterPro; IPR016167; FAD-bd_2_sub1.
InterPro; IPR002346; Mopterin_DH_FAD-bd.
InterPro; IPR022407; OxRdtase_Mopterin_BS.
InterPro; IPR014307; Xanthine_DH_ssu.
Pfam; PF01315; Ald_Xan_dh_C; 1.
Pfam; PF02738; Ald_Xan_dh_C2; 1.
Pfam; PF03450; CO_deh_flav_C; 1.
Pfam; PF00941; FAD_binding_5; 1.
Pfam; PF00111; Fer2; 1.
Pfam; PF01799; Fer2_2; 1.
PIRSF; PIRSF000127; Xanthine_DH; 1.
SMART; SM01008; Ald_Xan_dh_C; 1.
SMART; SM01092; CO_deh_flav_C; 1.
SUPFAM; SSF47741; SSF47741; 1.
SUPFAM; SSF54292; SSF54292; 1.
SUPFAM; SSF54665; SSF54665; 1.
SUPFAM; SSF55447; SSF55447; 1.
SUPFAM; SSF56003; SSF56003; 1.
SUPFAM; SSF56176; SSF56176; 1.
TIGRFAMs; TIGR02963; xanthine_xdhA; 1.
PROSITE; PS00197; 2FE2S_FER_1; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS51387; FAD_PCMH; 1.
PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
Glycoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD;
Oxidoreductase; Peroxisome; Reference proteome; Secreted.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7556219}.
CHAIN 2 1332 Xanthine dehydrogenase/oxidase.
/FTId=PRO_0000166082.
DOMAIN 4 91 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 229 414 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
NP_BIND 257 264 FAD. {ECO:0000269|PubMed:12421831,
ECO:0000269|PubMed:15148401}.
NP_BIND 347 351 FAD. {ECO:0000269|PubMed:12421831,
ECO:0000269|PubMed:15148401}.
ACT_SITE 1261 1261 Proton acceptor.
{ECO:0000269|PubMed:15148401}.
METAL 43 43 Iron-sulfur 1.
METAL 48 48 Iron-sulfur 1.
METAL 51 51 Iron-sulfur 1.
METAL 73 73 Iron-sulfur 1.
METAL 113 113 Iron-sulfur 2.
METAL 116 116 Iron-sulfur 2.
METAL 148 148 Iron-sulfur 2.
METAL 150 150 Iron-sulfur 2.
METAL 767 767 Molybdenum.
METAL 798 798 Molybdenum; via carbonyl oxygen.
METAL 912 912 Molybdenum; via amide nitrogen.
METAL 1079 1079 Molybdenum; via amide nitrogen.
BINDING 337 337 FAD. {ECO:0000269|PubMed:12421831,
ECO:0000269|PubMed:15148401}.
BINDING 360 360 FAD. {ECO:0000269|PubMed:12421831,
ECO:0000269|PubMed:15148401}.
BINDING 404 404 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:12421831,
ECO:0000269|PubMed:15148401}.
BINDING 422 422 FAD. {ECO:0000269|PubMed:12421831,
ECO:0000269|PubMed:15148401}.
BINDING 802 802 Substrate.
BINDING 880 880 Substrate.
BINDING 914 914 Substrate.
BINDING 1010 1010 Substrate; via amide nitrogen.
CARBOHYD 1073 1073 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 535 992 In oxidase form. {ECO:0000250}.
MUTAGEN 335 335 R->A: Promotes conversion to the oxidase
form that utilizes molecular oxygen as
electron acceptor. Interferes with normal
conversion to the dehydrogenase form by
reducing agents.
{ECO:0000269|PubMed:12817083}.
MUTAGEN 336 336 W->A: Promotes conversion to the oxidase
form that utilizes molecular oxygen as
electron acceptor. Interferes with normal
conversion to the dehydrogenase form by
reducing agents.
{ECO:0000269|PubMed:12817083}.
MUTAGEN 427 427 R->Q: Promotes conversion to the oxidase
form that utilizes molecular oxygen as
electron acceptor. Interferes with normal
conversion to the dehydrogenase form by
reducing agents.
{ECO:0000269|PubMed:12817083}.
CONFLICT 188 188 T -> TQ (in Ref. 2; CAA67117).
{ECO:0000305}.
CONFLICT 199 199 E -> K (in Ref. 2; CAA67117).
{ECO:0000305}.
CONFLICT 366 366 M -> V (in Ref. 2; CAA67117).
{ECO:0000305}.
CONFLICT 552 552 D -> H (in Ref. 1; CAA58497).
{ECO:0000305}.
CONFLICT 958 958 R -> K (in Ref. 2; CAA67117).
{ECO:0000305}.
CONFLICT 976 976 Q -> E (in Ref. 2; CAA67117).
{ECO:0000305}.
CONFLICT 1039 1040 GQ -> E (in Ref. 2; CAA67117).
{ECO:0000305}.
CONFLICT 1244 1244 L -> V (in Ref. 2; CAA67117).
{ECO:0000305}.
CONFLICT 1268 1268 A -> P (in Ref. 2; CAA67117).
{ECO:0000305}.
CONFLICT 1279 1281 RAA -> ARG (in Ref. 2; CAA67117).
{ECO:0000305}.
STRAND 6 10 {ECO:0000244|PDB:3NVW}.
STRAND 13 17 {ECO:0000244|PDB:3NVW}.
HELIX 26 32 {ECO:0000244|PDB:3NVW}.
STRAND 44 48 {ECO:0000244|PDB:3NVW}.
STRAND 52 59 {ECO:0000244|PDB:3NVW}.
TURN 60 63 {ECO:0000244|PDB:3NVW}.
STRAND 64 71 {ECO:0000244|PDB:3NVW}.
TURN 72 74 {ECO:0000244|PDB:3NVW}.
HELIX 77 79 {ECO:0000244|PDB:3NVW}.
STRAND 84 86 {ECO:0000244|PDB:3NVW}.
HELIX 88 90 {ECO:0000244|PDB:3NVW}.
STRAND 94 96 {ECO:0000244|PDB:1V97}.
HELIX 100 107 {ECO:0000244|PDB:3NVW}.
HELIX 117 130 {ECO:0000244|PDB:3NVW}.
HELIX 136 140 {ECO:0000244|PDB:3NVW}.
TURN 142 145 {ECO:0000244|PDB:3NVZ}.
STRAND 149 151 {ECO:0000244|PDB:3NVW}.
HELIX 154 161 {ECO:0000244|PDB:3NVW}.
HELIX 198 200 {ECO:0000244|PDB:3NVW}.
HELIX 206 208 {ECO:0000244|PDB:3UNC}.
HELIX 214 218 {ECO:0000244|PDB:3NVW}.
HELIX 219 221 {ECO:0000244|PDB:1FO4}.
STRAND 227 230 {ECO:0000244|PDB:3NVW}.
STRAND 235 238 {ECO:0000244|PDB:3NVW}.
HELIX 242 251 {ECO:0000244|PDB:3NVW}.
HELIX 264 270 {ECO:0000244|PDB:3NVW}.
STRAND 276 280 {ECO:0000244|PDB:3NVW}.
HELIX 285 287 {ECO:0000244|PDB:3NVW}.
STRAND 290 292 {ECO:0000244|PDB:3NVW}.
STRAND 294 300 {ECO:0000244|PDB:3NVW}.
HELIX 305 318 {ECO:0000244|PDB:3NVW}.
HELIX 321 323 {ECO:0000244|PDB:3NVW}.
HELIX 325 334 {ECO:0000244|PDB:3NVW}.
STRAND 336 338 {ECO:0000244|PDB:3EUB}.
HELIX 340 343 {ECO:0000244|PDB:3NVW}.
HELIX 348 354 {ECO:0000244|PDB:3NVW}.
HELIX 362 367 {ECO:0000244|PDB:3NVW}.
STRAND 371 376 {ECO:0000244|PDB:3NVW}.
STRAND 379 384 {ECO:0000244|PDB:3NVW}.
HELIX 387 389 {ECO:0000244|PDB:3NVW}.
STRAND 403 410 {ECO:0000244|PDB:3NVW}.
STRAND 416 422 {ECO:0000244|PDB:3NVW}.
STRAND 428 431 {ECO:0000244|PDB:3NVW}.
STRAND 435 443 {ECO:0000244|PDB:3NVW}.
STRAND 446 462 {ECO:0000244|PDB:3NVW}.
HELIX 467 471 {ECO:0000244|PDB:3NVW}.
TURN 472 475 {ECO:0000244|PDB:3NVW}.
STRAND 477 479 {ECO:0000244|PDB:3NVW}.
HELIX 480 493 {ECO:0000244|PDB:3NVW}.
HELIX 505 527 {ECO:0000244|PDB:3NVW}.
TURN 540 542 {ECO:0000244|PDB:3UNC}.
HELIX 543 546 {ECO:0000244|PDB:3UNC}.
STRAND 555 559 {ECO:0000244|PDB:3UNC}.
HELIX 582 586 {ECO:0000244|PDB:3NVW}.
HELIX 593 595 {ECO:0000244|PDB:3NVW}.
STRAND 603 609 {ECO:0000244|PDB:3NVW}.
STRAND 611 621 {ECO:0000244|PDB:3NVW}.
HELIX 625 627 {ECO:0000244|PDB:3NVW}.
STRAND 631 635 {ECO:0000244|PDB:3NVW}.
HELIX 637 639 {ECO:0000244|PDB:3NVW}.
STRAND 644 647 {ECO:0000244|PDB:3NVW}.
STRAND 652 655 {ECO:0000244|PDB:3NVW}.
STRAND 658 660 {ECO:0000244|PDB:3NVW}.
STRAND 666 674 {ECO:0000244|PDB:3NVW}.
HELIX 675 683 {ECO:0000244|PDB:3NVW}.
STRAND 686 691 {ECO:0000244|PDB:3NVW}.
HELIX 698 703 {ECO:0000244|PDB:3NVW}.
STRAND 707 717 {ECO:0000244|PDB:3NVW}.
HELIX 719 725 {ECO:0000244|PDB:3NVW}.
STRAND 727 736 {ECO:0000244|PDB:3NVW}.
STRAND 748 753 {ECO:0000244|PDB:3NVW}.
STRAND 760 764 {ECO:0000244|PDB:3NVW}.
HELIX 769 780 {ECO:0000244|PDB:3NVW}.
HELIX 784 786 {ECO:0000244|PDB:3NVW}.
STRAND 787 791 {ECO:0000244|PDB:3NVW}.
TURN 798 801 {ECO:0000244|PDB:3NVW}.
HELIX 806 819 {ECO:0000244|PDB:3NVW}.
STRAND 823 826 {ECO:0000244|PDB:3NVW}.
HELIX 829 835 {ECO:0000244|PDB:3NVW}.
STRAND 842 850 {ECO:0000244|PDB:3NVW}.
STRAND 856 866 {ECO:0000244|PDB:3NVW}.
HELIX 874 883 {ECO:0000244|PDB:3NVW}.
TURN 884 888 {ECO:0000244|PDB:3NVW}.
STRAND 892 901 {ECO:0000244|PDB:3NVW}.
TURN 912 915 {ECO:0000244|PDB:3NVW}.
HELIX 916 934 {ECO:0000244|PDB:3NVW}.
HELIX 938 945 {ECO:0000244|PDB:3NVW}.
HELIX 964 974 {ECO:0000244|PDB:3NVW}.
HELIX 977 990 {ECO:0000244|PDB:3NVW}.
STRAND 992 1008 {ECO:0000244|PDB:3NVW}.
HELIX 1012 1014 {ECO:0000244|PDB:3NVW}.
STRAND 1016 1023 {ECO:0000244|PDB:3NVW}.
STRAND 1029 1034 {ECO:0000244|PDB:3NVW}.
STRAND 1038 1040 {ECO:0000244|PDB:3NVW}.
HELIX 1042 1054 {ECO:0000244|PDB:3NVW}.
HELIX 1058 1060 {ECO:0000244|PDB:3NVW}.
STRAND 1061 1063 {ECO:0000244|PDB:3SR6}.
TURN 1068 1070 {ECO:0000244|PDB:3NVW}.
TURN 1079 1081 {ECO:0000244|PDB:3B9J}.
HELIX 1082 1107 {ECO:0000244|PDB:3NVW}.
HELIX 1113 1122 {ECO:0000244|PDB:3NVW}.
STRAND 1128 1134 {ECO:0000244|PDB:3NVW}.
TURN 1142 1145 {ECO:0000244|PDB:3NVW}.
STRAND 1151 1165 {ECO:0000244|PDB:3NVW}.
TURN 1166 1168 {ECO:0000244|PDB:3NVW}.
STRAND 1171 1181 {ECO:0000244|PDB:3NVW}.
HELIX 1188 1207 {ECO:0000244|PDB:3NVW}.
TURN 1224 1226 {ECO:0000244|PDB:3NVW}.
HELIX 1232 1234 {ECO:0000244|PDB:3NVW}.
STRAND 1237 1243 {ECO:0000244|PDB:3NVW}.
HELIX 1253 1255 {ECO:0000244|PDB:3NVW}.
HELIX 1264 1267 {ECO:0000244|PDB:3NVW}.
HELIX 1268 1285 {ECO:0000244|PDB:3NVW}.
HELIX 1302 1308 {ECO:0000244|PDB:3NVW}.
TURN 1312 1314 {ECO:0000244|PDB:3NVW}.
HELIX 1317 1319 {ECO:0000244|PDB:3NVW}.
SEQUENCE 1332 AA; 146790 MW; 744BA523471948B7 CRC64;
MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLRGTK LGCGEGGCGA CTVMLSKYDR
LQDKIIHFSA NACLAPICTL HHVAVTTVEG IGSTKTRLHP VQERIAKSHG SQCGFCTPGI
VMSMYTLLRN QPEPTVEEIE DAFQGNLCRC TGYRPILQGF RTFAKNGGCC GGNGNNPNCC
MNQKKDHTVT LSPSLFNPEE FMPLDPTQEP IFPPELLRLK DVPPKQLRFE GERVTWIQAS
TLKELLDLKA QHPEAKLVVG NTEIGIEMKF KNQLFPMIIC PAWIPELNAV EHGPEGISFG
AACALSSVEK TLLEAVAKLP TQKTEVFRGV LEQLRWFAGK QVKSVASLGG NIITASPISD
LNPVFMASGT KLTIVSRGTR RTVPMDHTFF PSYRKTLLGP EEILLSIEIP YSREDEFFSA
FKQASRREDD IAKVTCGMRV LFQPGSMQVK ELALCYGGMA DRTISALKTT QKQLSKFWNE
KLLQDVCAGL AEELSLSPDA PGGMIEFRRT LTLSFFFKFY LTVLKKLGKD SKDKCGKLDP
TYTSATLLFQ KDPPANIQLF QEVPNGQSKE DTVGRPLPHL AAAMQASGEA VYCDDIPRYE
NELFLRLVTS TRAHAKIKSI DVSEAQKVPG FVCFLSADDI PGSNETGLFN DETVFAKDTV
TCVGHIIGAV VADTPEHAER AAHVVKVTYE DLPAIITIED AIKNNSFYGS ELKIEKGDLK
KGFSEADNVV SGELYIGGQD HFYLETHCTI AIPKGEEGEM ELFVSTQNAM KTQSFVAKML
GVPVNRILVR VKRMGGGFGG KETRSTLVSV AVALAAYKTG HPVRCMLDRN EDMLITGGRH
PFLARYKVGF MKTGTIVALE VDHYSNAGNS RDLSHSIMER ALFHMDNCYK IPNIRGTGRL
CKTNLSSNTA FRGFGGPQAL FIAENWMSEV AVTCGLPAEE VRWKNMYKEG DLTHFNQRLE
GFSVPRCWDE CLKSSQYYAR KSEVDKFNKE NCWKKRGLCI IPTKFGISFT VPFLNQAGAL
IHVYTDGSVL VSHGGTEMGQ GLHTKMVQVA SKALKIPISK IYISETSTNT VPNSSPTAAS
VSTDIYGQAV YEACQTILKR LEPFKKKNPD GSWEDWVMAA YQDRVSLSTT GFYRTPNLGY
SFETNSGNAF HYFTYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
QGLGLFTLEE LHYSPEGSLH TRGPSTYKIP AFGSIPTEFR VSLLRDCPNK KAIYASKAVG
EPPLFLGASV FFAIKDAIRA ARAQHTNNNT KELFRLDSPA TPEKIRNACV DKFTTLCVTG
APGNCKPWSL RV


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