› 1h23

X-ray diffraction
2.15Å resolution

Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with (S,S)-(-)-bis(12)-hupyridone at 2.15A resolution

Released:
DOI: 10.2210/pdb1h23/pdb
PDB entry 1h23 coloured by chain, front view.
PDB entry 1h23 coloured by chain, side view.
PDB entry 1h23 coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Acetylcholinesterase complexed with bivalent ligands related to huperzine a: experimental evidence for species-dependent protein-ligand complementarity.
Wong DM, Greenblatt HM, Dvir H, Carlier PR, Han YF, Pang YP, Silman I, Sussman JL
J Am Chem Soc 125 363-73 (2003)
PMID: 12517147

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: 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

2 bound ligands:
Ligand E12 1 x E12
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P3121
Unit cell:
a: 111.794Å b: 111.794Å c: 137.775Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.189 0.215

Quick links

Citations

7 review citations

Recent advances in the multitarget-directed ligands approach for the treatment of Alzheimer's disease.
León et al. (2013)
6 more

12 mentions without citation

CSAR benchmark exercise of 2010: selection of the protein-ligand complexes.
Dunbar et al. (2011)
11 more