PDBe 4eyw

X-ray diffraction
1.88Å resolution

Crystal structure of rat carnitine palmitoyltransferase 2 in complex with 1-[(R)-2-(3,4-Dihydro-1H-isoquinoline-2-carbonyl)-piperidin-1-yl]-2-phenoxy-ethanone

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carnitine O-palmitoyltransferase 2, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 634 amino acids
Theoretical weight: 71.53 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

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P42212
Unit cell:
a: 148.144Å b: 148.144Å c: 192.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.197
Expression system: Escherichia coli BL21(DE3)