Structure of PDB 3oid Chain A

Receptor sequence

>3oidA (length=249) Species: 1423 (Bacillus subtilis)

QNKCALVTGSSRGVGKAAAIRLAENGYNIVINYARSKKAALETAEEIEKL
GVKVLVVKANVGQPAKIKEMFQQIDETFGRLDVFVNNAASGVLRPVMELE
ETHWDWTMNINAKALLFCAQEAAKLMEKNGGGHIVSISSLGSIRYLENYT
TVGVSKAALEALTRYLAVELSPKQIIVNAVSGGAIDTDALKHFPNREDLL
EDARQNTPAGRMVEIKDMVDTVEFLVSSKADMIRGQTIIVDGGRSLLVL

3D structure

• PDB: 3oid Crystal Structures of Enoyl-ACP Reductases I (FabI) and III (FabL) from B. subtilis
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G15 S141 Y151 V154 K158
• Catalytic site (residue number reindexed from 1): G13 S139 Y149 V152 K156
• Enzyme Commision number: 1.3.1.104: enoyl-[acyl-carrier-protein] reductase.

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	TCL	A	S92 G93 Y151 A191 H194 F195	S90 G91 Y149 A189 H192 F193
BS02	NDP	A	G11 S13 R14 G15 V16 A36 R37 S38 A61 N62 V63 N89 A90 A91 I112 I139 S140 S141 K158 G184 A186 I187 T189 A191	G9 S11 R12 G13 V14 A34 R35 S36 A59 N60 V61 N87 A88 A89 I110 I137 S138 S139 K156 G182 A184 I185 T187 A189

Gene Ontology

Molecular Function

• GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
• GO:0016491 oxidoreductase activity
• GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
• GO:0050661 NADP binding
• GO:0141148 enoyl-[acyl-carrier-protein] reductase (NADPH) activity

Biological Process

• GO:0006633 fatty acid biosynthetic process
• GO:0030497 fatty acid elongation

External links

• PDB: RCSB:3oid, PDBe:3oid, PDBj:3oid
• PDBsum: 3oid
• PubMed: 21185310
• UniProt: P71079|FABL_BACSU Enoyl-[acyl-carrier-protein] reductase [NADPH] FabL (Gene Name=fabL)