› 5dlp

X-ray diffraction
2.7Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 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, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
3 bound ligands:
Ligand MBT 1 x MBT
Ligand NAG 1 x NAG
Ligand SO4 15 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3121
Unit cell:
a: 111.059Å b: 111.059Å c: 137.172Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.193 0.224

Quick links

Citations

3 review citations

Detect, correct, retract: How to manage incorrect structural models.
Wlodawer et al. (2018)
2 more

2 mentions without citation

The impact of crystallization conditions on structure-based drug design: A case study on the methylene blue/acetylcholinesterase complex.
Dym et al. (2016)
1 more