5end

X-ray diffraction
2.55Å resolution

Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(Q152A) from Vibrio cholerae

Released:

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:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-192033 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] reductase FabG Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 26.03 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KQH7 (Residues: 1-244; Coverage: 100%)
Gene names: VC_2021, fabG
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P62
Unit cell:
a: 63.995Å b: 63.995Å c: 190.474Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.206 0.255
Expression system: Escherichia coli