6f25

X-ray diffraction
3.05Å resolution

Crystal structure of human acetylcholinesterase in complex with C35.

Released:

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 (3 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 539 amino acids
Theoretical weight: 59.1 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P22303 (Residues: 36-574; Coverage: 93%)
Gene name: ACHE
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer : NEW Components: NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P61
Unit cell:
a: 211.074Å b: 211.074Å c: 115.725Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.178 0.214
Expression system: Cricetulus griseus