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4EUE

Crystal structure of Clostridium acetobutulicum trans-2-enoyl-CoA reductase in complex with NADH

Functional Information from GO Data
ChainGOidnamespacecontents
A0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016628molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
A0050343molecular_functiontrans-2-enoyl-CoA reductase (NADH) activity
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NAI A 1001
ChainResidue
AGLY47
AGLU110
AASP111
AALA112
ASER138
ALEU139
AALA140
AALA141
ATYR223
ASER224
ATYR225
AALA48
ALYS244
ALYS272
AALA273
ALEU274
ATHR276
AALA278
ASER279
APHE285
ANA1002
AHOH1150
ASER49
AHOH1166
AHOH1167
AHOH1192
AHOH1253
AHOH1258
ASER50
AGLY51
APHE52
ASER73
ATYR74
AGLU75

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1002
ChainResidue
AGLY47
ASER50
APHE52
AGLY53
ASER138
ANAI1001

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01838","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23050861","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23050861","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Plays an important role in discriminating NADH against NADPH","evidences":[{"source":"PubMed","id":"23050861","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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