PDBe 2h3p

X-ray diffraction
2.2Å resolution

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

Released:
Source organism: Mus musculus

Function and Biology Details

Reaction catalysed:
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
Macromolecule:
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
UniProt:
  • Canonical: P47934 (Residues: 30-625; Coverage: 95%)
Gene name: Crat
Sequence domains: Choline/Carnitine o-acyltransferase

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 163.9Å b: 89.24Å c: 122.64Å
α: 90° β: 128.96° γ: 90°
R-values:
R R work R free
0.17 0.17 0.223
Expression system: Escherichia coli