Structure of PDB 3oif Chain D

Receptor sequence
>3oifD (length=257) Species: 1423 (Bacillus subtilis) [Search protein sequence]
MNFSLEGRNIVVMGVANKRSIAWGIARSLHEAGARLIFTYAGERLEKSVH
ELAGTLDRNDSIILPCDVTNDAEIETCFASIKEQVGVIHGIAHCIAFANK
EELVGEYLNTNRDGFLLAHNISSYSLTAVVKAARPMMTEGGSIVTLTYLG
GELVMPNYNVMGVAKASLDASVKYLAADLGKENIRVNSISAGPIRTLSAK
GSDFNSILKDIEERAPLRRTTTPEEVGDTAAFLFSDMSRGITGENLHVDS
GFHITAR
3D structure
PDB3oif Crystal Structures of Enoyl-ACP Reductases I (FabI) and III (FabL) from B. subtilis
ChainD
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y148 Y158 M161 K165 K200
Catalytic site (residue number reindexed from 1) Y148 Y158 M161 K165 K200
Enzyme Commision number 1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD D G14 V15 S20 I21 A41 D67 V68 C94 I95 A96 L146 T147 Y148 K165 A191 P193 I194 T196 S198 G14 V15 S20 I21 A41 D67 V68 C94 I95 A96 L146 T147 Y148 K165 A191 P193 I194 T196 S198
BS02 TCL D A96 A98 Y148 Y158 S198 A96 A98 Y148 Y158 S198 BindingDB: IC50=500nM
Gene Ontology
Molecular Function
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0030497 fatty acid elongation
GO:0070417 cellular response to cold

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Molecular Function
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Biological Process
External links
PDB RCSB:3oif, PDBe:3oif, PDBj:3oif
PDBsum3oif
PubMed21185310
UniProtP54616|FABI_BACSU Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (Gene Name=fabI)

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