1q83

X-ray diffraction
2.65Å resolution

Crystal structure of the mouse acetylcholinesterase-TZ2PA6 syn complex

Released:
Source organism: Mus musculus
Primary publication:
Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation.
Proc. Natl. Acad. Sci. U.S.A. 101 1449-54 (2004)
PMID: 14757816

Function and Biology Details

Reaction catalysed:
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

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: 580 amino acids
Theoretical weight: 63.8 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 1-580; Coverage: 94%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUL
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 79.743Å b: 111.954Å c: 226.577Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.221
Expression system: Homo sapiens