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3OIC

Crystal Structure of Enoyl-ACP Reductases III (FabL) from B. subtilis (apo form)

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
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0030497biological_processfatty acid elongation
A0050661molecular_functionNADP binding
A0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
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
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0030497biological_processfatty acid elongation
D0050661molecular_functionNADP binding
D0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 259
ChainResidue
DASP84
DASN131
DGLY132
DGLY133
DGLY134
DHOH299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21185310","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21185310","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3OID","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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