2h3w

X-ray diffraction
2.1Å resolution

Crystal structure of the S554A/M564G mutant of murine carnitine acetyltransferase in complex with hexanoylcarnitine and CoA

Released:
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
Macromolecule:
Carnitine O-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 599 amino acids
Theoretical weight: 67.95 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
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 164.06Å b: 89.07Å c: 122.78Å
α: 90° β: 128.97° γ: 90°
R-values:
R R work R free
0.177 0.177 0.219
Expression system: Escherichia coli