2cek

X-ray diffraction
2.2Å resolution

Conformational Flexibility in the Peripheral Site of Torpedo californica Acetylcholinesterase Revealed by the Complex Structure with a Bifunctional Inhibitor

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 535 amino acids
Theoretical weight: 60.56 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 22-556; Coverage: 95%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: Rossmann fold

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P3121
Unit cell:
a: 111.94Å b: 111.94Å c: 137.12Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.175 0.206