3OIC

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
A	0006633	biological_process	fatty acid biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0030497	biological_process	fatty acid elongation
A	0050661	molecular_function	NADP binding
A	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
D	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
D	0006633	biological_process	fatty acid biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0030497	biological_process	fatty acid elongation
D	0050661	molecular_function	NADP binding
D	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 259

Chain	Residue
D	ASP84
D	ASN131
D	GLY132
D	GLY133
D	GLY134
D	HOH299

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:21185310

Chain	Residue	Details
A	TYR151
A	LYS158
D	TYR151
D	LYS158

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site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:21185310, ECO:0007744|PDB:3OID

Chain	Residue	Details
A	SER13
D	ASN89
D	LYS158
D	ILE187
A	ALA36
A	ASN62
A	ASN89
A	LYS158
A	ILE187
D	SER13
D	ALA36
D	ASN62

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