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2E1Q

Crystal Structure of Human Xanthine Oxidoreductase mutant, Glu803Val

Functional Information from GO Data
ChainGOidnamespacecontents
A0000255biological_processallantoin metabolic process
A0004854molecular_functionxanthine dehydrogenase activity
A0004855molecular_functionxanthine oxidase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein 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
A0016226biological_processiron-sulfur cluster assembly
A0016491molecular_functionoxidoreductase activity
A0016529cellular_componentsarcoplasmic reticulum
A0030856biological_processregulation of epithelial cell differentiation
A0042803molecular_functionprotein homodimerization activity
A0043546molecular_functionmolybdopterin cofactor binding
A0043605biological_processamide catabolic process
A0046038biological_processGMP catabolic process
A0046055biological_processdGMP catabolic process
A0046059biological_processdAMP catabolic process
A0046872molecular_functionmetal ion binding
A0050660molecular_functionflavin adenine dinucleotide binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
A0070674molecular_functionhypoxanthine dehydrogenase activity
A0070675molecular_functionhypoxanthine oxidase activity
A0071949molecular_functionFAD binding
B0000255biological_processallantoin metabolic process
B0004854molecular_functionxanthine dehydrogenase activity
B0004855molecular_functionxanthine oxidase activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0006147biological_processguanine catabolic process
B0006148biological_processinosine catabolic process
B0006149biological_processdeoxyinosine catabolic process
B0006154biological_processadenosine catabolic process
B0006157biological_processdeoxyadenosine catabolic process
B0006161biological_processdeoxyguanosine catabolic process
B0006196biological_processAMP catabolic process
B0006204biological_processIMP catabolic process
B0007595biological_processlactation
B0009114biological_processhypoxanthine catabolic process
B0009115biological_processxanthine catabolic process
B0016226biological_processiron-sulfur cluster assembly
B0016491molecular_functionoxidoreductase activity
B0016529cellular_componentsarcoplasmic reticulum
B0030856biological_processregulation of epithelial cell differentiation
B0042803molecular_functionprotein homodimerization activity
B0043546molecular_functionmolybdopterin cofactor binding
B0043605biological_processamide catabolic process
B0046038biological_processGMP catabolic process
B0046055biological_processdGMP catabolic process
B0046059biological_processdAMP catabolic process
B0046872molecular_functionmetal ion binding
B0050660molecular_functionflavin adenine dinucleotide binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
B0070674molecular_functionhypoxanthine dehydrogenase activity
B0070675molecular_functionhypoxanthine oxidase activity
B0071949molecular_functionFAD binding
C0000255biological_processallantoin metabolic process
C0004854molecular_functionxanthine dehydrogenase activity
C0004855molecular_functionxanthine oxidase activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005737cellular_componentcytoplasm
C0005777cellular_componentperoxisome
C0005829cellular_componentcytosol
C0006147biological_processguanine catabolic process
C0006148biological_processinosine catabolic process
C0006149biological_processdeoxyinosine catabolic process
C0006154biological_processadenosine catabolic process
C0006157biological_processdeoxyadenosine catabolic process
C0006161biological_processdeoxyguanosine catabolic process
C0006196biological_processAMP catabolic process
C0006204biological_processIMP catabolic process
C0007595biological_processlactation
C0009114biological_processhypoxanthine catabolic process
C0009115biological_processxanthine catabolic process
C0016226biological_processiron-sulfur cluster assembly
C0016491molecular_functionoxidoreductase activity
C0016529cellular_componentsarcoplasmic reticulum
C0030856biological_processregulation of epithelial cell differentiation
C0042803molecular_functionprotein homodimerization activity
C0043546molecular_functionmolybdopterin cofactor binding
C0043605biological_processamide catabolic process
C0046038biological_processGMP catabolic process
C0046055biological_processdGMP catabolic process
C0046059biological_processdAMP catabolic process
C0046872molecular_functionmetal ion binding
C0050660molecular_functionflavin adenine dinucleotide binding
C0051536molecular_functioniron-sulfur cluster binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
C0070674molecular_functionhypoxanthine dehydrogenase activity
C0070675molecular_functionhypoxanthine oxidase activity
C0071949molecular_functionFAD binding
D0000255biological_processallantoin metabolic process
D0004854molecular_functionxanthine dehydrogenase activity
D0004855molecular_functionxanthine oxidase activity
D0005506molecular_functioniron ion binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005737cellular_componentcytoplasm
D0005777cellular_componentperoxisome
D0005829cellular_componentcytosol
D0006147biological_processguanine catabolic process
D0006148biological_processinosine catabolic process
D0006149biological_processdeoxyinosine catabolic process
D0006154biological_processadenosine catabolic process
D0006157biological_processdeoxyadenosine catabolic process
D0006161biological_processdeoxyguanosine catabolic process
D0006196biological_processAMP catabolic process
D0006204biological_processIMP catabolic process
D0007595biological_processlactation
D0009114biological_processhypoxanthine catabolic process
D0009115biological_processxanthine catabolic process
D0016226biological_processiron-sulfur cluster assembly
D0016491molecular_functionoxidoreductase activity
D0016529cellular_componentsarcoplasmic reticulum
D0030856biological_processregulation of epithelial cell differentiation
D0042803molecular_functionprotein homodimerization activity
D0043546molecular_functionmolybdopterin cofactor binding
D0043605biological_processamide catabolic process
D0046038biological_processGMP catabolic process
D0046055biological_processdGMP catabolic process
D0046059biological_processdAMP catabolic process
D0046872molecular_functionmetal ion binding
D0050660molecular_functionflavin adenine dinucleotide binding
D0051536molecular_functioniron-sulfur cluster binding
D0051537molecular_function2 iron, 2 sulfur cluster binding
D0070674molecular_functionhypoxanthine dehydrogenase activity
D0070675molecular_functionhypoxanthine oxidase activity
D0071949molecular_functionFAD binding
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. GFggKvtrstvvstava..LaayKTgrpVrCmlDRdeD
ChainResidueDetails
AGLY798-ASP833

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues348
DetailsDomain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues740
DetailsDomain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues56
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues56
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17301077","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Human milk xanthine dehydrogenase is incompletely converted to the oxidase form in the absence of proteolysis. A structural explanation.","authors":["Pearson A.R.","Godber B.L.J.","Eisenthal R.","Taylor G.L.","Harrison R."]}}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fiq
ChainResidueDetails
AGLU1262

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fiq
ChainResidueDetails
BGLU1262

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fiq
ChainResidueDetails
CGLU1262

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fiq
ChainResidueDetails
DGLU1262

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1fiq
ChainResidueDetails
AGLN768
AARG913

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1fiq
ChainResidueDetails
BGLN768
BARG913

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1fiq
ChainResidueDetails
CGLN768
CARG913

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1fiq
ChainResidueDetails
DGLN768
DARG913

238895

PDB entries from 2025-07-16

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