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3AN1

Crystal structure of rat D428A mutant, urate bound form

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
B0000255biological_processallantoin metabolic process
B0001933biological_processnegative regulation of protein phosphorylation
B0001937biological_processnegative regulation of endothelial cell proliferation
B0004854molecular_functionxanthine dehydrogenase activity
B0004855molecular_functionxanthine oxidase activity
B0005506molecular_functioniron ion 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
B0010044biological_processresponse to aluminum ion
B0010629biological_processnegative regulation of gene expression
B0016226biological_processiron-sulfur cluster assembly
B0016491molecular_functionoxidoreductase activity
B0016529cellular_componentsarcoplasmic reticulum
B0030856biological_processregulation of epithelial cell differentiation
B0032496biological_processresponse to lipopolysaccharide
B0034465biological_processresponse to carbon monoxide
B0042542biological_processresponse to hydrogen peroxide
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043546molecular_functionmolybdopterin cofactor binding
B0043605biological_processamide catabolic process
B0045602biological_processnegative regulation of endothelial cell differentiation
B0046038biological_processGMP catabolic process
B0046055biological_processdGMP catabolic process
B0046059biological_processdAMP catabolic process
B0046872molecular_functionmetal ion binding
B0050421molecular_functionnitrite reductase (NO-forming) activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
B0051898biological_processnegative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B0070674molecular_functionhypoxanthine dehydrogenase activity
B0070675molecular_functionhypoxanthine oxidase activity
B0071347biological_processcellular response to interleukin-1
B0071356biological_processcellular response to tumor necrosis factor
B0071949molecular_functionFAD binding
B0097184biological_processresponse to azide
B1900745biological_processpositive regulation of p38MAPK cascade
B1900747biological_processnegative regulation of vascular endothelial growth factor signaling pathway
B2000379biological_processpositive regulation of reactive oxygen species metabolic process
B2001213biological_processnegative regulation of vasculogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 3001
ChainResidue
AGLN111
ACYS112
AGLY113
ACYS115
ACYS147
AARG148
ACYS149
ALEU744

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FES A 3002
ChainResidue
ACYS43
AGLY44
AGLY46
AGLY47
ACYS48
AGLY49
ACYS51
AASN71
ACYS73
AGLY42

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1332
ChainResidue
AGLU740
AHIS741
ATYR743
ATHR836
AGLY837
AHOH1482

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 4009
ChainResidue
AGLY867
ATHR870
AGLU871
ASER874
ASER907
AASN908

site_idAC5
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 3006
ChainResidue
AGLU45
AGLY46
ALYS255
ALEU256
AVAL257
AVAL258
AGLY259
AASN260
ATHR261
AGLU262
AILE263
AALA300
APHE336
AALA337
AVAL341
ASER346
AGLY349
AASN350
AILE352
ATHR353
ASER358
AASP359
AILE402
ALEU403
ALYS421
AASP429
AHOH1414
AHOH1826
AHOH1916
AHOH2052
AHOH2076
AHOH2340

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE URC A 1333
ChainResidue
AGLU802
AARG880
APHE914
APHE1009
ATHR1010
AALA1078
AALA1079
AGLU1261
AHOH1581
AHOH1744
AHOH2262

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCT A 1334
ChainResidue
AARG839
AHIS840
AILE877
ATHR909
AALA910
APHE911
APHE914
AGLY915
AGLN918

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1335
ChainResidue
AGLN561
AGLY574
ASER1184
ASER1185
AHOH1710
AHOH2010

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES B 4001
ChainResidue
BGLN111
BCYS112
BGLY113
BCYS115
BCYS147
BARG148
BCYS149
BLEU744

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FES B 4002
ChainResidue
BGLY46
BGLY47
BCYS48
BGLY49
BCYS51
BASN71
BCYS73
BGLY42
BCYS43
BGLY44

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 4019
ChainResidue
BGLY867
BTHR870
BGLU871
BASP872
BSER874
BSER907
BASN908

site_idBC3
Number of Residues31
DetailsBINDING SITE FOR RESIDUE FAD B 4006
ChainResidue
BGLU45
BGLY46
BLEU256
BVAL257
BVAL258
BGLY259
BASN260
BTHR261
BGLU262
BILE263
BALA300
BPHE336
BALA337
BALA345
BSER346
BGLY349
BASN350
BILE352
BTHR353
BSER358
BASP359
BLEU403
BLYS421
BASP429
BHOH1642
BHOH1666
BHOH1864
BHOH1868
BHOH1944
BHOH2271
BHOH2544

site_idBC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE URC B 1332
ChainResidue
BGLU802
BARG880
BPHE914
BSER1008
BPHE1009
BTHR1010
BALA1078
BALA1079
BGLU1261
BHOH1858
BHOH2074
BHOH2398

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BCT B 1333
ChainResidue
BARG839
BHIS840
BILE877
BTHR909
BALA910
BPHE911
BPHE914
BGLY915
BGLN918

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1334
ChainResidue
BGLN561
BGLY574
BSER1184
BSER1185
BHOH1871
BHOH2426

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1335
ChainResidue
BGLU740
BHIS741
BTYR743
BTHR836
BGLY837
BHOH1392

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 Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU1261
BGLU1261

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:17301076, ECO:0007744|PDB:2E3T
ChainResidueDetails
ACYS43
BCYS48
BCYS51
BCYS73
BCYS112
BCYS115
BCYS147
BCYS149
ACYS48
ACYS51
ACYS73
ACYS112
ACYS115
ACYS147
ACYS149
BCYS43

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076
ChainResidueDetails
ALEU256
ASER346
AASP359
ALEU403
BLEU256
BSER346
BASP359
BLEU403

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
APHE336
BGLN767
BPHE798
BARG912
BPHE914
BALA1079
ALYS421
AGLN767
APHE798
AARG912
APHE914
AALA1079
BPHE336
BLYS421

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AGLU802
AARG880
ATHR1010
BGLU802
BARG880
BTHR1010

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PDB entries from 2024-05-01

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