Function and Biology Details
Reaction catalysed:
Palmitoyl-[protein] + H(2)O = palmitate + [protein]
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Palmitoyl thioesterase CPT1C (preferred)
PDBe Complex ID:
PDB-CPX-186192 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Palmitoyl thioesterase CPT1C
Molecule details ›
Chain: A
Length: 50 amino acids
Theoretical weight: 5.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Carnitine O-palmitoyltransferase N-terminus
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 50 amino acids
Theoretical weight: 5.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8TCG5 (Residues: 1-50; Coverage: 6%)
Sequence domains: Carnitine O-palmitoyltransferase N-terminus
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
24%
Refinement method:
simulated annealing
Expression system: Escherichia coli
