› 4moc

X-ray diffraction
2.5Å resolution

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + H(2)O = CoA + acetate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186801 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-coenzyme A thioesterase Chain: A
Molecule details ›
Chain: A
Length: 332 amino acids
Theoretical weight: 37.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8WYK0 (Residues: 7-336; Coverage: 60%)
Gene names: ACOT12, CACH, CACH1, STARD15
Sequence domains: Thioesterase superfamily
Structure domains: Hotdog Thioesterase

Ligands and Environments


Cofactor: Ligand COA 1 x COA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P321
Unit cell:
a: 123.56Å b: 123.56Å c: 49.75Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.202 0.247
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Deactivating Fatty Acids: Acyl-CoA Thioesterase-Mediated Control of Lipid Metabolism.
Tillander et al. (2017)
1 more

3 mentions without citation

Structural basis for regulation of the human acetyl-CoA thioesterase 12 and interactions with the steroidogenic acute regulatory protein-related lipid transfer (START) domain.
Swarbrick et al. (2014)
2 more