X-ray diffraction
2.9Å resolution

Crystal Structure of Human Acetylcholinesterase

Source organism: Homo sapiens
Entry authors: Dym O, Unger T, Toker L, Silman I, Sussman JL, Israel Structural Proteomics Center (ISPC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 543 amino acids
Theoretical weight: 59.58 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
  • Canonical: P22303 (Residues: 32-574; Coverage: 93%)
Gene name: ACHE
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P3112
Unit cell:
a: 125.307Å b: 125.307Å c: 131.396Å
α: 90° β: 90° γ: 120°
R R work R free
0.187 0.185 0.218
Expression system: Homo sapiens