1hnd

X-ray diffraction
1.6Å resolution

CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX

Released:
Source organism: Escherichia coli

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO(2) 
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] synthase 3 Chain: A
Molecule details ›
Chain: A
Length: 317 amino acids
Theoretical weight: 33.55 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6R0 (Residues: 1-317; Coverage: 100%)
Gene names: JW1077, b1091, fabH
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments


Cofactor: Ligand COA 1 x COA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P41212
Unit cell:
a: 72.51Å b: 72.51Å c: 102.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.257
Expression system: Escherichia coli