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1SIQ

The Crystal Structure and Mechanism of Human Glutaryl-CoA Dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE FAD A 399
ChainResidue
APHE133
AGLN277
APHE278
ALEU282
AASN285
AGLN286
AASP343
AMET344
AGLY346
AGLY347
AILE350
ALEU135
ATYR369
ATHR372
APHE390
AHOH401
AHOH404
AHOH406
AHOH407
AHOH423
AHOH424
AHOH425
ATHR136
AGLY141
ASER142
ATRP168
ATHR170
ALEU212
AARG275

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
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
AGLU370

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AARG94
APHE133
ASER142
ATRP168
APHE243
AGLY371
ATHR372
APHE390

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG275
AGLN286
AASP343

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q60759
ChainResidueDetails
ALYS196

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

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PDB entries from 2024-07-17

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