› 1ndi

X-ray diffraction
2.3Å resolution

Carnitine Acetyltransferase in complex with CoA

Released:
DOI: 10.2210/pdb1ndi/pdb
PDB entry 1ndi coloured by chain, front view.
PDB entry 1ndi coloured by chain, side view.
PDB entry 1ndi coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport.
Jogl G, Tong L
Cell 112 113-22 (2003)
PMID: 12526798

Function and Biology Details

Reactions catalysed: 
Octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
Acetyl-CoA + carnitine = CoA + O-acetylcarnitine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carnitine O-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 596 amino acids
Theoretical weight: 67.68 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P47934 (Residues: 30-625; Coverage: 95%)
Gene name: Crat
Sequence domains: Choline/Carnitine o-acyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand COA 2 x COA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 162.26Å b: 92.05Å c: 122.9Å
α: 90° β: 128.98° γ: 90°
R-values:
R R work R free
0.27 0.27 0.363
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Lipid metabolic enzymes: emerging drug targets for the treatment of obesity.
Shi et al. (2004)
16 more

6 mentions without citation

Combining specificity determining and conserved residues improves functional site prediction.
Kalinina et al. (2009)
5 more