› 2fyo

X-ray diffraction
2Å resolution

Crystal structure of rat carnitine palmitoyltransferase 2 in space group P43212

Released:
DOI: 10.2210/pdb2fyo/pdb
PDB entry 2fyo coloured by chain, front view.
PDB entry 2fyo coloured by chain, side view.
PDB entry 2fyo coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
A monotopic membrane protein goes solo.
Mattevi A
Structure 14 628-9 (2006)
PMID: 16615901

Function and Biology Details

Reaction catalysed: 
Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148462 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carnitine O-palmitoyltransferase 2, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 653 amino acids
Theoretical weight: 74.13 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P18886 (Residues: 27-658; Coverage: 96%)
Gene names: Cpt-2, Cpt2
Sequence domains: Choline/Carnitine o-acyltransferase
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P43212
Unit cell:
a: 67.55Å b: 67.55Å c: 307.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.179 0.235
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Monotopic Membrane Proteins Join the Fold.
Allen et al. (2019)
2 other articles

1 mention without citation

Small Molecule Inhibitors of Metabolic Enzymes Repurposed as a New Class of Anthelmintics.
Tyagi et al. (2018)