› 2le3

Solution NMR

N-terminal regulatory segment of carnitine palmitoyltransferase 1A

Released:
DOI: 10.2210/pdb2le3/pdb
PDB entry 2le3 coloured by chain, ensemble of 20 models, front view.
PDB entry 2le3 coloured by chain, ensemble of 20 models, side view.
PDB entry 2le3 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
An environment-dependent structural switch underlies the regulation of carnitine palmitoyltransferase 1A.
Rao JN, Warren GZL, Estolt-Povedano S, Zammit VA, Ulmer TS
J Biol Chem 286 42545-42554 (2011)
PMID: 21990363

Function and Biology Details

Reaction catalysed: 
Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156178 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carnitine O-palmitoyltransferase 1, liver isoform Chain: A
Molecule details ›
Chain: A
Length: 42 amino acids
Theoretical weight: 4.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50416 (Residues: 1-42; Coverage: 5%)
Gene names: CPT1, CPT1A
Sequence domains: Carnitine O-palmitoyltransferase N-terminus

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 63%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Carnitine palmitoyltransferase 1C: From cognition to cancer.
Casals et al. (2016)
4 more

4 mentions without citation

Telomerase structure.
Sandin et al. (2014)
3 more