› 1u65

X-ray diffraction
2.61Å 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
Macromolecules (4 distinct):
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 543 amino acids
Theoretical weight: 61.33 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 22-564; Coverage: 96%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUL
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
3 bound ligands:
Ligand NAG 2 x NAG
Ligand CP0 1 x CP0
Ligand IOD 1 x IOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P3221
Unit cell:
a: 137.87Å b: 137.87Å c: 70.89Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.187 0.237

Quick links

Citations

2 review citations

FOLFIRINOX for locally advanced and metastatic pancreatic cancer: single institution retrospective review of efficacy and toxicity.
Gunturu et al. (2013)
1 more

4 mentions without citation

Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site.
Harel et al. (2008)
3 more