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1WYG

Crystal Structure of a Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000255biological_processallantoin metabolic process
A0001933biological_processnegative regulation of protein phosphorylation
A0001937biological_processnegative regulation of endothelial cell proliferation
A0004854molecular_functionxanthine dehydrogenase activity
A0004855molecular_functionxanthine oxidase activity
A0005506molecular_functioniron ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0006147biological_processguanine catabolic process
A0006148biological_processinosine catabolic process
A0006149biological_processdeoxyinosine catabolic process
A0006154biological_processadenosine catabolic process
A0006157biological_processdeoxyadenosine catabolic process
A0006161biological_processdeoxyguanosine catabolic process
A0006196biological_processAMP catabolic process
A0006204biological_processIMP catabolic process
A0007595biological_processlactation
A0009114biological_processhypoxanthine catabolic process
A0009115biological_processxanthine catabolic process
A0010044biological_processresponse to aluminum ion
A0010629biological_processnegative regulation of gene expression
A0016226biological_processiron-sulfur cluster assembly
A0016491molecular_functionoxidoreductase activity
A0016529cellular_componentsarcoplasmic reticulum
A0030856biological_processregulation of epithelial cell differentiation
A0032496biological_processresponse to lipopolysaccharide
A0034465biological_processresponse to carbon monoxide
A0042542biological_processresponse to hydrogen peroxide
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043546molecular_functionmolybdopterin cofactor binding
A0043605biological_processamide catabolic process
A0045602biological_processnegative regulation of endothelial cell differentiation
A0046038biological_processGMP catabolic process
A0046055biological_processdGMP catabolic process
A0046059biological_processdAMP catabolic process
A0046872molecular_functionmetal ion binding
A0050421molecular_functionnitrite reductase (NO-forming) activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
A0051898biological_processnegative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0070674molecular_functionhypoxanthine dehydrogenase activity
A0070675molecular_functionhypoxanthine oxidase activity
A0071347biological_processcellular response to interleukin-1
A0071356biological_processcellular response to tumor necrosis factor
A0071949molecular_functionFAD binding
A0097184biological_processresponse to azide
A1900745biological_processpositive regulation of p38MAPK cascade
A1900747biological_processnegative regulation of vascular endothelial growth factor signaling pathway
A2000379biological_processpositive regulation of reactive oxygen species metabolic process
A2001213biological_processnegative regulation of vasculogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 2001
ChainResidue
AGLN1040
ASER1080
ASER1082
AALA1083
AACY3001

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 2002
ChainResidue
APRO937
AALA938
ALYS981
AASP1276

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 2003
ChainResidue
ATHR611
AARG612

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 4001
ChainResidue
AGLY867
ATHR870
AGLU871
AASP872
ASER874
ASER907
AASN908

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES A 4002
ChainResidue
AGLN111
ACYS112
ACYS115
ACYS147
AARG148
ACYS149
ALEU744

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FES A 4003
ChainResidue
AGLY42
ACYS43
AGLY44
AGLY46
AGLY47
ACYS48
AGLY49
ACYS51
AASN71
ACYS73

site_idAC7
Number of Residues29
DetailsBINDING SITE FOR RESIDUE FAD A 4004
ChainResidue
AGLU45
AGLY46
ALYS255
ALEU256
AVAL257
AVAL258
AGLY259
AASN260
ATHR261
AGLU262
AILE263
AALA300
ATRP335
APHE336
AALA337
AVAL341
AALA345
ASER346
AGLY349
AASN350
AILE352
ATHR353
ASER358
AASP359
AILE402
ALEU403
ALYS421
AASP428
AASP429

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SAL A 4005
ChainResidue
AGLU802
AARG880
APHE914
APHE1009
ATHR1010
AALA1078
AALA1079
AGLU1261

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 3001
ChainResidue
AALA1078
AALA1079
ASER1080
APO42001

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CGEGGCGAC
ChainResidueDetails
ACYS43-CYS51

site_idPS00559
Number of Residues36
DetailsMOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. GFggKetrstvvstala..LaahKTgrpVrCmlDRdeD
ChainResidueDetails
AGLY797-ASP832

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
APRO1262

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17301076, ECO:0007744|PDB:2E3T
ChainResidueDetails
AGLY44
AGLY49
ATHR52
ALEU74
AGLY113
ATHR116
AARG148
ATHR150

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076
ChainResidueDetails
AVAL257
AILE347
ALEU360
ALEU404

site_idSWS_FT_FI4
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AALA337
AGLN422
AASN768
AGLY799
AGLY913
AGLY915
ASER1080

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ATHR803
AALA881
ALEU1011

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fiq
ChainResidueDetails
AGLU1261

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1fiq
ChainResidueDetails
AARG912
AGLN767

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PDB entries from 2024-07-24

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