7UM8

Crystal structure of E. Coli FabI in complex with NAD and (R,E)-3-(7-amino-8-oxo-6,7,8,9-tetrahydro-5H-pyrido[2,3-b]azepin-3-yl)-N-methyl-N-((3-methylbenzofuran-2-yl)methyl)acrylamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006633	biological_process	fatty acid biosynthetic process
A	0008610	biological_process	lipid biosynthetic process
A	0009102	biological_process	biotin biosynthetic process
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0030497	biological_process	fatty acid elongation
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0046677	biological_process	response to antibiotic
A	0051289	biological_process	protein homotetramerization
A	0070404	molecular_function	NADH binding
A	1902494	cellular_component	catalytic complex
B	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0006633	biological_process	fatty acid biosynthetic process
B	0008610	biological_process	lipid biosynthetic process
B	0009102	biological_process	biotin biosynthetic process
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0030497	biological_process	fatty acid elongation
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0046677	biological_process	response to antibiotic
B	0051289	biological_process	protein homotetramerization
B	0070404	molecular_function	NADH binding
B	1902494	cellular_component	catalytic complex

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269\|PubMed:10201369, ECO:0000269\|PubMed:10398587, ECO:0000269\|PubMed:10493822, ECO:0000269\|PubMed:10595560, ECO:0000269\|PubMed:11514139, ECO:0000269\|PubMed:12109908, ECO:0000269\|PubMed:12699381, ECO:0000269\|PubMed:8953047

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Involved in acyl-ACP binding

Catalytic Information from CSA

Chain	Residue	Details
A	TYR156	proton acceptor, proton donor
A	LYS163	electrostatic stabiliser

Chain	Residue	Details
B	TYR156	proton acceptor, proton donor
B	LYS163	electrostatic stabiliser