› 1qti

X-ray diffraction
2.5Å resolution

Function and Biology Details

Reaction catalysed: 
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 537 amino acids
Theoretical weight: 60.74 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 22-558; Coverage: 95%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand GNT 1 x GNT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P3121
Unit cell:
a: 110.824Å b: 110.824Å c: 136.445Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.192 0.236

Quick links

Citations

13 review citations

Cholinesterases, a target of pharmacology and toxicology.
Pohanka M. (2011)
12 more

20 mentions without citation

Limitations in current acetylcholinesterase structure-based design of oxime antidotes for organophosphate poisoning.
Kovalevsky et al. (2016)
19 more