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1SIR

The Crystal Structure and Mechanism of Human Glutaryl-CoA Dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000062molecular_functionfatty-acyl-CoA binding
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0004361molecular_functionglutaryl-CoA dehydrogenase activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006568biological_processL-tryptophan metabolic process
A0006637biological_processacyl-CoA metabolic process
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0019395biological_processfatty acid oxidation
A0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
A0046949biological_processfatty-acyl-CoA biosynthetic process
A0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD A 399
ChainResidue
APHE133
AARG275
APHE278
ALEU282
AASN285
AGLN286
AASP343
AMET344
AGLY347
AILE350
ATHR372
ALEU135
APHE390
ANBC400
AHOH501
AHOH502
AHOH506
ATHR136
AGLY141
ASER142
ATRP168
AILE169
ATHR170
ALEU212

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NBC A 400
ChainResidue
AARG94
ASER95
ALEU103
ASER142
APRO144
ATHR170
APHE243
AGLY244
ALEU246
AASN247
AARG250
APRO320
ATYR369
AGLU370
AARG382
AFAD399

Functional Information from PROSITE/UniProt
site_idPS00072
Number of Residues13
DetailsACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. GLTEpnSGSDpsS
ChainResidueDetails
AGLY134-SER146

site_idPS00073
Number of Residues20
DetailsACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. DmLGGnGIsdEyhviRhamN
ChainResidueDetails
AASP343-ASN362

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q60759","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
AALA249

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ivh
ChainResidueDetails
AGLU370

242500

PDB entries from 2025-10-01

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