› 1q7b

X-ray diffraction
2.05Å resolution

The structure of betaketoacyl-[ACP] reductase from E. coli in complex with NADP+

Released:
DOI: 10.2210/pdb1q7b/pdb
PDB entry 1q7b coloured by chain, front view.
PDB entry 1q7b coloured by chain, side view.
PDB entry 1q7b coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG.
Price AC, Zhang YM, Rock CO, White SW
Structure 12 417-28 (2004)
PMID: 15016358

Function and Biology Details

Reaction catalysed: 
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142471 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] reductase FabG Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 244 amino acids
Theoretical weight: 25.59 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEK2 (Residues: 1-244; Coverage: 100%)
Gene names: JW1079, b1093, fabG
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAP 4 x NAP
1 bound ligand:
Ligand CA 8 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P21
Unit cell:
a: 72.748Å b: 76.182Å c: 99.733Å
α: 90° β: 109.47° γ: 90°
R-values:
R R work R free
0.201 0.2 0.221
Expression system: Escherichia coli

Quick links

Citations

12 review citations

The structural biology of type II fatty acid biosynthesis.
White et al. (2005)
11 more

24 mentions without citation

Fatty acid biosynthesis revisited: structure elucidation and metabolic engineering.
Beld et al. (2015)
23 more