› 1nm8

X-ray diffraction
1.6Å resolution

Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer

Released:
DOI: 10.2210/pdb1nm8/pdb
PDB entry 1nm8 coloured by chain, front view.
PDB entry 1nm8 coloured by chain, side view.
PDB entry 1nm8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer.
Wu D, Govindasamy L, Lian W, Gu Y, Kukar T, Agbandje-McKenna M, McKenna R
J Biol Chem 278 13159-65 (2003)
PMID: 12562770

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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 137.5Å b: 84.5Å c: 57.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.232
Expression system: Escherichia coli

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Citations

11 review citations

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Weng et al. (2010)
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6 mentions without citation

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Drecourt et al. (2018)
5 more