› 1ndb

X-ray diffraction
1.8Å resolution

Crystal structure of Carnitine Acetyltransferase

Released:
DOI: 10.2210/pdb1ndb/pdb
PDB entry 1ndb coloured by chain, front view.
PDB entry 1ndb coloured by chain, side view.
PDB entry 1ndb 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: 68.62 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

No bound ligands
1 modified residue:
Ligand MSE 40 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 158.884Å b: 89.654Å c: 119.436Å
α: 90° β: 127.46° γ: 90°
R-values:
R R work R free
0.192 0.192 0.219
Expression system: Escherichia coli

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Citations

15 review citations

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

5 mentions without citation

Monotopic Membrane Proteins Join the Fold.
Allen et al. (2019)
4 more