› 1s5o

X-ray diffraction
1.8Å resolution

Structural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase

Released:
DOI: 10.2210/pdb1s5o/pdb
PDB entry 1s5o coloured by chain, front view.
PDB entry 1s5o coloured by chain, side view.
PDB entry 1s5o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase.
Govindasamy L, Kukar T, Lian W, Pedersen B, Gu Y, Agbandje-McKenna M, Jin S, McKenna R, Wu D
J Struct Biol 146 416-24 (2004)
PMID: 15099582

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-154961 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carnitine O-acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 616 amino acids
Theoretical weight: 69.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P43155 (Residues: 35-626; Coverage: 95%)
Gene names: CAT1, CRAT
Sequence domains: Choline/Carnitine o-acyltransferase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 152 1 x 152
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 137.56Å b: 84.65Å c: 57.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.189 not available
Expression system: Escherichia coli

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Citations

1 review citation

Structural insight into function and regulation of carnitine palmitoyltransferase.
Rufer et al. (2009)
11 other articles