› 1q84

X-ray diffraction
2.45Å resolution

Crystal structure of the mouse acetylcholinesterase-TZ2PA6 anti complex

Released:
DOI: 10.2210/pdb1q84/pdb
PDB entry 1q84 coloured by chain, front view.
PDB entry 1q84 coloured by chain, side view.
PDB entry 1q84 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
Macromolecule:
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

3 bound ligands:
Ligand NAG 2 x NAG
Ligand P6G 1 x P6G
Ligand TZ4 2 x TZ4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 79.272Å b: 111.765Å c: 227.171Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.184 0.214
Expression system: Homo sapiens

Quick links

Citations

22 review citations

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

12 mentions without citation

Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation.
Bourne et al. (2004)
11 more