› 1q83

X-ray diffraction
2.65Å resolution

Crystal structure of the mouse acetylcholinesterase-TZ2PA6 syn complex

Released:
DOI: 10.2210/pdb1q83/pdb
PDB entry 1q83 coloured by chain, front view.
PDB entry 1q83 coloured by chain, side view.
PDB entry 1q83 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation.
Bourne Y, Kolb HC, Radić Z, Sharpless KB, Taylor P, Marchot P
Proc Natl Acad Sci U S A 101 1449-54 (2004)
PMID: 14757816

Function and Biology Details

Reaction catalysed: 
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149441 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 580 amino acids
Theoretical weight: 63.8 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 1-580; Coverage: 94%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUL
Carbohydrate polymer
3 bound ligands:
Ligand NAG 2 x NAG
Ligand P6G 1 x P6G
Ligand TZ5 2 x TZ5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 79.743Å b: 111.954Å c: 226.577Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.182 0.221
Expression system: Homo sapiens

Quick links

Citations

22 review citations

Fragment-based lead discovery.
Rees et al. (2004)
21 more

14 mentions without citation

A perspective on multi-target drug discovery and design for complex diseases.
Ramsay et al. (2018)
13 more