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2R0N

The effect of a Glu370Asp mutation in Glutaryl-CoA Dehydrogenase on Proton Transfer to the Dienolate Intermediate

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_processtryptophan 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 Residues27
DetailsBINDING SITE FOR RESIDUE FAD A 400
ChainResidue
APHE133
AARG275
APHE278
AASN285
AGLN286
AASP343
AMET344
AGLY347
AILE350
ATYR369
AGLU370
ALEU135
ATHR372
AASP374
APHE390
AHOH502
AHOH505
AHOH510
AHOH521
AHOH551
ATHR136
AGLY141
ASER142
ATRP168
AILE169
ATHR170
ALEU212

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE TGC A 500
ChainResidue
AARG94
ASER95
ASER98
AGLY141
ASER142
APRO144
AGLY240
APHE243
ALEU246
AASN247
AARG250
APRO320
ATYR369
AGLU370
AILE379
AARG382
APHE390
AHOH503
AHOH537
AHOH584
AHOH594

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 2024-05-01

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