3ftp

X-ray diffraction
2.05Å resolution

Crystal structure of 3-Ketoacyl-(acyl-carrier-protein) reductase from Burkholderia pseudomallei at 2.05 A resolution

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-174658 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 270 amino acids
Theoretical weight: 28.09 KDa
Source organism: Burkholderia pseudomallei
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3JQ67 (Residues: 1-249; Coverage: 100%)
Gene names: BURPS1710b_2905, fabG
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 86.62Å b: 89.9Å c: 120.24Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.268
Expression system: Escherichia coli