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4UHW

Human aldehyde oxidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004031molecular_functionaldehyde oxidase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006805biological_processxenobiotic metabolic process
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043546molecular_functionmolybdopterin cofactor binding
A0046872molecular_functionmetal ion binding
A0050660molecular_functionflavin adenine dinucleotide binding
A0051287molecular_functionNAD binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
A0070062cellular_componentextracellular exosome
A0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 3001
ChainResidue
AGLN113
ACYS114
AGLY115
ACYS117
ACYS149
AARG150
ACYS151
AMET753

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 3002
ChainResidue
ACYS44
AGLY45
AGLY47
ACYS49
AGLY50
ACYS52
ACYS74
AGLY43

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE MTE A 3003
ChainResidue
AGLN113
ACYS151
AGLY805
AALA806
APHE807
AARG921
AMET1047
AGLY1048
AGLN1049
AGLY1087
AGLY1088
ASER1089
AVAL1090
AVAL1091
AALA1092
AGLN1203
ALEU1268
AMOS3004

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MOS A 3004
ChainResidue
AGLN776
AGLY808
APHE920
AARG921
AGLY1087
AGLY1088
AGLU1270
AMTE3003

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD A 3006
ChainResidue
AGLY46
AGLY47
APRO263
AVAL264
AMET266
AGLY267
AASN268
ATHR269
ASER270
AVAL271
ALEU344
AALA345
AALA353
ASER354
AGLY357
AHIS358
AILE360
ASER361
AHIS363
ASER366
AASP367
AILE410
ALEU411
ALEU438

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MLI A 2337
ChainResidue
AARG32
ALYS33
ATHR38
AASP601
AMET603
ALEU605
AARG833
AHOH2019

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MLI A 2338
ChainResidue
ACYS44
AGLY48
ACYS49
ALEU148
AARG433
APHE751
ATYR1236
ALYS1237
AILE1238

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CGGGGCGAC
ChainResidueDetails
ACYS44-CYS52

site_idPS00559
Number of Residues36
DetailsMOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. AFggKvlktgiiaavta..FaanKHgraVrCvlERgeD
ChainResidueDetails
AALA806-ASP841

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor; for azaheterocycle hydroxylase activity => ECO:0000250|UniProtKB:O54754
ChainResidueDetails
AGLU1270

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26322824, ECO:0007744|PDB:4UHW
ChainResidueDetails
ACYS44

site_idSWS_FT_FI3
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:26322824, ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG
ChainResidueDetails
ACYS49
AASP367
ALEU411
AALA806
AMET1047
AGLY1088
AGLN1203
ACYS52
ACYS74
ACYS114
ACYS117
ACYS149
ACYS151
AVAL264
ASER354

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26322824, ECO:0007744|PDB:4UHW, ECO:0007744|PDB:4UHX
ChainResidueDetails
AGLN113
AALA345

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26322824, ECO:0000269|PubMed:26842593, ECO:0007744|PDB:5EPG
ChainResidueDetails
AHIS358

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26322824, ECO:0007744|PDB:4UHX
ChainResidueDetails
ALEU1268

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER1068

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PDB entries from 2024-07-24

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