X-ray diffraction
2.8Å resolution

Crystal structure of a potent and reversible dual binding site Acetylcholinesterase chiral inhibitor


Function and Biology Details

Reaction catalysed:
Acetylcholine + H(2)O = choline + acetate

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 572 amino acids
Theoretical weight: 65.32 KDa
Source organism: Tetronarce californica
Expression system: Tetronarce californica
  • Canonical: P04058 (Residues: 25-556; Coverage: 94%)
  • Best match: P04058-2 (Residues: 25-596)
Gene name: ache
Sequence domains: Carboxylesterase family

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3121
Unit cell:
a: 111.42Å b: 111.42Å c: 137.37Å
α: 90° β: 90° γ: 120°
R R work R free
0.191 0.188 0.235
Expression system: Tetronarce californica