› 2rcu

X-ray diffraction
1.78Å resolution

Crystal structure of rat carnitine palmitoyltransferase 2 in complex with r-3-(hexadecanoylamino)-4-(trimethylazaniumyl)butanoate

Released:
DOI: 10.2210/pdb2rcu/pdb
PDB entry 2rcu coloured by chain, front view.
PDB entry 2rcu coloured by chain, side view.
PDB entry 2rcu coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Carnitine palmitoyltransferase 2: analysis of membrane association and complex structure with a substrate analog.
Rufer AC, Lomize A, Benz J, Chomienne O, Thoma R, Hennig M
FEBS Lett 581 3247-52 (2007)
PMID: 17585909

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 653 amino acids
Theoretical weight: 73.57 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P18886 (Residues: 27-658; Coverage: 96%)
Gene names: Cpt-2, Cpt2
Sequence domains: Choline/Carnitine o-acyltransferase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand BOG 1 x BOG
Ligand BUJ 2 x BUJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 95.273Å b: 97.75Å c: 312.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.177 0.223
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Structures of membrane proteins.
Vinothkumar et al. (2010)
3 more

2 mentions without citation

Identification of a residue affecting fatty alcohol selectivity in wax ester synthase.
Barney et al. (2013)
1 more