2ha0

X-ray diffraction
2.2Å resolution

Crystal structure of mouse acetylcholinesterase complexed with 4-ketoamyltrimethylammonium

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 (2 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 543 amino acids
Theoretical weight: 59.76 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 32-574; Coverage: 93%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 79.228Å b: 111.795Å c: 226.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.219
Expression system: Homo sapiens