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8EMT

Cryo-EM analysis of the human aldehyde oxidase from liver

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
B0004031molecular_functionaldehyde oxidase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006805biological_processxenobiotic metabolic process
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043546molecular_functionmolybdopterin cofactor binding
B0046872molecular_functionmetal ion binding
B0050660molecular_functionflavin adenine dinucleotide binding
B0051287molecular_functionNAD binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
B0070062cellular_componentextracellular exosome
B0071949molecular_functionFAD binding
Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CGGGGCGAC
ChainResidueDetails
BCYS44-CYS52

site_idPS00559
Number of Residues36
DetailsMOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. AFggKvlktgiiaavta..FaanKHgraVrCvlERgeD
ChainResidueDetails
BALA806-ASP841

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor; for azaheterocycle hydroxylase activity => ECO:0000250|UniProtKB:O54754
ChainResidueDetails
BGLU1270
AGLU1270

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26322824, ECO:0007744|PDB:4UHW
ChainResidueDetails
BCYS44
ACYS44

site_idSWS_FT_FI3
Number of Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:26322824, ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG
ChainResidueDetails
BCYS49
BASP367
BLEU411
BALA806
BMET1047
BGLY1088
BGLN1203
ACYS49
ACYS52
ACYS74
ACYS114
BCYS52
ACYS117
ACYS149
ACYS151
AVAL264
ASER354
AASP367
ALEU411
AALA806
AMET1047
AGLY1088
BCYS74
AGLN1203
BCYS114
BCYS117
BCYS149
BCYS151
BVAL264
BSER354

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:26322824, ECO:0007744|PDB:4UHW, ECO:0007744|PDB:4UHX
ChainResidueDetails
BGLN113
BALA345
AGLN113
AALA345

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26322824, ECO:0000269|PubMed:26842593, ECO:0007744|PDB:5EPG
ChainResidueDetails
BHIS358
AHIS358

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26322824, ECO:0007744|PDB:4UHX
ChainResidueDetails
BLEU1268
ALEU1268

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER1068
ASER1068

226707

PDB entries from 2024-10-30

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