› 2iwy

X-ray diffraction
2.06Å resolution

Human mitochondrial beta-ketoacyl ACP synthase

Released:
DOI: 10.2210/pdb2iwy/pdb
PDB entry 2iwy coloured by chain, front view.
PDB entry 2iwy coloured by chain, side view.
PDB entry 2iwy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase.
Christensen CE, Kragelund BB, von Wettstein-Knowles P, Henriksen A
Protein Sci 16 261-72 (2007)
PMID: 17242430

Function and Biology Details

Reaction catalysed: 
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192662 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 438 amino acids
Theoretical weight: 46.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli M15
UniProt:
  • Canonical: Q9NWU1 (Residues: 38-459; Coverage: 92%)
Gene name: OXSM
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
Ligand NH4 2 x NH4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P212121
Unit cell:
a: 72.626Å b: 96.061Å c: 115.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.205
Expression system: Escherichia coli M15

Quick links

Citations

5 review citations

Current understanding of fatty acid biosynthesis and the acyl carrier protein.
Chan et al. (2010)
4 more

3 mentions without citation

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