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4JQC

Crystal Structure of E.coli Enoyl Reductase in Complex with NAD and AFN-1252

Functional Information from GO Data
ChainGOidnamespacecontents
A0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0008610biological_processlipid biosynthetic process
A0009102biological_processbiotin biosynthetic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0030497biological_processfatty acid elongation
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046677biological_processresponse to antibiotic
A0051289biological_processprotein homotetramerization
A0070404molecular_functionNADH binding
A1902494cellular_componentcatalytic complex
B0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0008610biological_processlipid biosynthetic process
B0009102biological_processbiotin biosynthetic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0030497biological_processfatty acid elongation
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0046677biological_processresponse to antibiotic
B0051289biological_processprotein homotetramerization
B0070404molecular_functionNADH binding
B1902494cellular_componentcatalytic complex
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAD A 301
ChainResidue
AGLY13
AILE92
AGLY93
AILE119
ALEU144
ASER145
ALYS163
AALA189
AGLY190
AILE192
ATHR194
AALA15
ALEU195
AALA196
A0WE302
AILE20
AGLN40
ALEU44
ACYS63
AASP64
AVAL65
ASER91

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 0WE A 302
ChainResidue
APHE94
AALA95
AGLY97
ATYR146
AASN155
ATYR156
AALA196
ASER198
AILE200
ANAD301

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAD B 301
ChainResidue
BGLY13
BVAL14
BSER19
BILE20
BGLN40
BLEU44
BCYS63
BASP64
BVAL65
BSER91
BILE92
BGLY93
BILE119
BSER145
BLYS163
BALA189
BGLY190
BILE192
BTHR194
BLEU195
BALA196
B0WE302

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 0WE B 302
ChainResidue
BPHE94
BALA95
BGLY97
BASN155
BTYR156
BSER198
BGLY199
BNAD301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10201369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10398587","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10493822","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10595560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11514139","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12109908","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12699381","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8953047","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsSite: {"description":"Involved in acyl-ACP binding"}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 606
ChainResidueDetails
ATYR156proton acceptor, proton donor
ALYS163electrostatic stabiliser

site_idMCSA2
Number of Residues2
DetailsM-CSA 606
ChainResidueDetails
BTYR156proton acceptor, proton donor
BLYS163electrostatic stabiliser

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PDB entries from 2025-10-15

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