Structure of PDB 4bo2 Chain D

Receptor sequence
>4bo2D (length=245) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
LYFQSMSLQGKVALVTGASRGIGQAIALELGRLGAVVIGTATSASGAEKI
AETLKANGVEGAGLVLDVSSDESVAATLEHIQQHLGQPLIVVNNAGIRMK
DDEWFDVVNTNLNSLYRLSKAVLRGMTKARWGRIINIGSVVGAMGNAGQT
NYAAAKAGLEGFTRALAREVGSRAITVNAVAPGFIDTDMTRELPEAQREA
LLGQIPLGRLGQAEEIAKVVGFLASDGAAYVTGATVPVNGGMYMS
3D structure
PDB4bo2 Discovery of an Allosteric Inhibitor Binding Site in 3-Oxo-Acyl-Acp Reductase from Pseudomonas Aeruginosa
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) G16 S141 Y154 K158
Catalytic site (residue number reindexed from 1) G21 S139 Y152 K156
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 36K D W106 F107 N111 A156 G160 G163 F164 W104 F105 N109 A154 G158 G161 F162
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4bo2, PDBe:4bo2, PDBj:4bo2
PDBsum4bo2
PubMed24015914
UniProtO54438|FABG_PSEAE 3-oxoacyl-[acyl-carrier-protein] reductase FabG (Gene Name=fabG)

[Back to BioLiP]