Structure of PDB 3oid Chain D

Receptor sequence

>3oidD (length=248) Species: 1423 (Bacillus subtilis)

NKCALVTGSSRGVGKAAAIRLAENGYNIVINYARSKKAALETAEEIEKLG
VKVLVVKANVGQPAKIKEMFQQIDETFGRLDVFVNNAASGVLRPVMELEE
THWDWTMNINAKALLFCAQEAAKLMEKNGGGHIVSISSLGSIRYLENYTT
VGVSKAALEALTRYLAVELSPKQIIVNAVSGGAIDTDALKHFPNREDLLE
DARQNTPAGRMVEIKDMVDTVEFLVSSKADMIRGQTIIVDGGRSLLVL

3D structure

• PDB: 3oid Crystal Structures of Enoyl-ACP Reductases I (FabI) and III (FabL) from B. subtilis
• Chain: D
• 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): G12 S138 Y148 V151 K155
• 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	D	A91 S92 G93 Y151 A191 H194 F195	A88 S89 G90 Y148 A188 H191 F192
BS02	NDP	D	G11 S13 R14 G15 V16 A36 R37 S38 A61 N62 V63 N89 A90 A91 I112 I139 S140 S141 K158 A186 I187 T189 A191	G8 S10 R11 G12 V13 A33 R34 S35 A58 N59 V60 N86 A87 A88 I109 I136 S137 S138 K155 A183 I184 T186 A188

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)