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3OIG

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0030497biological_processfatty acid elongation
A0070417biological_processcellular response to cold
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAD A 1501
ChainResidue
AGLY14
ATHR69
ACYS94
AILE95
AALA96
ALEU146
ATHR147
ALYS165
AALA191
AGLY192
APRO193
AVAL15
AILE194
ATHR196
ALEU197
ASER198
AHOH271
AHOH274
AHOH276
AHOH282
AIMJ301
AHOH487
AALA16
AHOH500
AHOH501
ASER20
AILE21
AALA41
ACYS66
AASP67
AVAL68

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IMJ A 301
ChainResidue
APHE97
AALA98
ATYR148
AASN157
ATYR158
ASER198
AILE202
AHOH299
AHOH384
ANAD1501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ATYR148

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR158

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21185310
ChainResidueDetails
AGLY14
ASER20
AASP67
AILE95
ALYS165
AILE194

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AALA98

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Involved in acyl-ACP binding => ECO:0000250
ChainResidueDetails
AASN206

223166

PDB entries from 2024-07-31

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