Structure of PDB 4bnu Chain D

Receptor sequence
>4bnuD (length=246) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
LYFQSMSLQGKVALVTGASRGIGQAIALELGRLGAVVIGTATSASGAEKI
AETLKANGVEGAGLVLDVSSDESVAATLEHIQQHLGQPLIVVNNAGIVRM
KDDEWFDVVNTNLNSLYRLSKAVLRGMTKARWGRIINIGSVVGAMGNAGQ
TNYAAAKAGLEGFTRALAREVGSRAITVNAVAPGFIDTDMTRELPEAQRE
ALLGQIPLGRLGQAEEIAKVVGFLASDGAAYVTGATVPVNGGMYMS
3D structure
PDB4bnu Discovery of an Allosteric Inhibitor Binding Site in 3-Oxo-Acyl-Acp Reductase from Pseudomonas Aeruginosa
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G16 S141 Y154 K158
Catalytic site (residue number reindexed from 1) G21 S140 Y153 K157
Enzyme Commision number 1.1.1.100: 3-oxoacyl-[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 9KQ D F107 V110 N111 L114 G160 G163 F164 F106 V109 N110 L113 G159 G162 F163 MOAD: ic50=0.02uM
Gene Ontology
Molecular Function
GO:0004316 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) 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:0051287 NAD binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0030497 fatty acid elongation

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Molecular Function
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Biological Process
External links
PDB RCSB:4bnu, PDBe:4bnu, PDBj:4bnu
PDBsum4bnu
PubMed24015914
UniProtO54438|FABG_PSEAE 3-oxoacyl-[acyl-carrier-protein] reductase FabG (Gene Name=fabG)

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