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4EUF

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

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 Residues23
DetailsBINDING SITE FOR RESIDUE NAD A 1001
ChainResidue
AGLY47
AGLU110
AALA112
ALEU139
AALA140
AALA141
ATYR223
ASER224
ATYR235
ALYS244
ALYS272
AALA48
ALEU274
APHE285
ANA1002
AHOH1114
ASER49
ASER50
AGLY51
APHE52
ASER73
ATYR74
AGLU75

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1002
ChainResidue
AGLY47
ASER50
APHE52
AGLY53
ASER138
ANAD1001

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

242500

PDB entries from 2025-10-01

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