› 3i6m

X-ray diffraction
2.26Å resolution

3D Structure of Torpedo californica acetylcholinesterase complexed with N-piperidinopropyl-galanthamine

Released:
DOI: 10.2210/pdb3i6m/pdb
PDB entry 3i6m coloured by chain, front view.
PDB entry 3i6m coloured by chain, side view.
PDB entry 3i6m coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Probing Torpedo californica acetylcholinesterase catalytic gorge with two novel bis-functional galanthamine derivatives.
Bartolucci C, Haller LA, Jordis U, Fels G, Lamba D
J Med Chem 53 745-51 (2010)
PMID: 20025280

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 (2 distinct):
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 534 amino acids
Theoretical weight: 60.45 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 23-556; Coverage: 95%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 1 x NAG
Ligand G3X 1 x G3X
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P3121
Unit cell:
a: 112.194Å b: 112.194Å c: 137.194Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.213

Quick links

Citations

2 review citations

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

6 mentions without citation

A Review on Recent Approaches on Molecular Docking Studies of Novel Compounds Targeting Acetylcholinesterase in Alzheimer Disease.
Peitzika et al. (2023)
5 more