X-ray diffraction
1.9Å resolution

Crystal structure of murine carnitine acetyltransferase in complex with carnitine and CoA

Source organism: Mus musculus

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Carnitine O-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 599 amino acids
Theoretical weight: 68.04 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
  • 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
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 164.51Å b: 89.74Å c: 122.95Å
α: 90° β: 128.96° γ: 90°
R R work R free
0.193 0.193 0.235
Expression system: Escherichia coli