› 2j3q

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reaction catalysed: 
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137374 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 543 amino acids
Theoretical weight: 61.33 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 22-564; Coverage: 96%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand TFL 1 x TFL
Ligand NAG 3 x NAG
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 139.44Å b: 139.44Å c: 71.42Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.199 0.257

Quick links

Citations

9 review citations

Why has butyrylcholinesterase been retained? Structural and functional diversification in a duplicated gene.
Johnson et al. (2012)
8 more

9 mentions without citation

Molecular mechanism of Thioflavin-T binding to amyloid fibrils.
Biancalana et al. (2010)
8 more