X-ray diffraction
3.2Å resolution

Recombinant human acetylcholinesterase

Source organism: Homo sapiens
Primary publication:
Acetylcholinesterase: from 3D structure to function.
Chem. Biol. Interact. 187 10-22 (2010)
PMID: 20138030

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 540 amino acids
Theoretical weight: 59.23 KDa
Source organism: Homo sapiens
Expression system: Drosophila
  • Canonical: P22303 (Residues: 35-574; Coverage: 93%)
Gene name: ACHE
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P61
Unit cell:
a: 210.9Å b: 210.9Å c: 115.27Å
α: 90° β: 90° γ: 120°
R R work R free
0.179 0.176 0.22
Expression system: Drosophila