1i01

X-ray diffraction
2.6Å resolution

CRYSTAL STRUCTURE OF BETA-KETOACYL [ACYL CARRIER PROTEIN] REDUCTASE FROM E. COLI.

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:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
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, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 61.7Å b: 120.1Å c: 131.1Å
α: 90° β: 90.5° γ: 90°
R-values:
R R work R free
0.229 0.228 0.25
Expression system: Escherichia coli