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3OIF

Crystal Structure of Enoyl-ACP Reductases I (FabI) from B. subtilis (complex with NAD and TCL)

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
A0030497biological_processfatty acid elongation
A0070417biological_processcellular response to cold
B0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0030497biological_processfatty acid elongation
B0070417biological_processcellular response to cold
C0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006633biological_processfatty acid biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0030497biological_processfatty acid elongation
C0070417biological_processcellular response to cold
D0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006633biological_processfatty acid biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0030497biological_processfatty acid elongation
D0070417biological_processcellular response to cold
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAD A 501
ChainResidue
AGLY14
AVAL68
ACYS94
AILE95
AALA96
ALEU146
ATHR147
ATYR148
ALYS165
AALA191
APRO193
AVAL15
AILE194
ATHR196
ALEU197
ASER198
AHOH298
ATCL502
AALA16
ASER20
AILE21
AALA41
ALEU45
ACYS66
AASP67

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TCL A 502
ChainResidue
AALA96
AALA98
ATYR148
ATYR158
AMET161
ASER198
AILE202
ANAD501

site_idAC3
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAD D 601
ChainResidue
DGLY14
DVAL15
DSER20
DILE21
DALA41
DLEU45
DCYS66
DASP67
DVAL68
DTHR69
DCYS94
DILE95
DALA96
DLEU146
DTHR147
DTYR148
DLYS165
DALA191
DGLY192
DPRO193
DILE194
DTHR196
DLEU197
DSER198
DHOH290
DHOH294
DTCL602

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TCL D 602
ChainResidue
DALA96
DALA98
DTYR148
DTYR158
DMET161
DSER198
DNAD601

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21185310","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Involved in acyl-ACP binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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