› 1hnd

X-ray diffraction
1.6Å resolution

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

Released:
DOI: 10.2210/pdb1hnd/pdb
PDB entry 1hnd coloured by chain, front view.
PDB entry 1hnd coloured by chain, side view.
PDB entry 1hnd coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Refined structures of beta-ketoacyl-acyl carrier protein synthase III.
Qiu X, Janson CA, Smith WW, Head M, Lonsdale J, Konstantinidis AK
J Mol Biol 307 341-56 (2001)
PMID: 11243824

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141418 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-ketoacyl-[acyl-carrier-protein] synthase III 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

Quick links

Citations

13 review citations

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

5 mentions without citation

Structural classification and properties of ketoacyl synthases.
Chen et al. (2011)
4 more