› 2ha2

X-ray diffraction
2.05Å resolution

Crystal structure of mouse acetylcholinesterase complexed with succinylcholine

Released:
DOI: 10.2210/pdb2ha2/pdb
PDB entry 2ha2 coloured by chain, front view.
PDB entry 2ha2 coloured by chain, side view.
PDB entry 2ha2 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding.
Bourne Y, Radic Z, Sulzenbacher G, Kim E, Taylor P, Marchot P
J Biol Chem 281 29256-67 (2006)
PMID: 16837465

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-149441 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 543 amino acids
Theoretical weight: 59.76 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 32-574; Coverage: 93%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
5 bound ligands:
Ligand FUC 1 x FUC
Ligand NAG 2 x NAG
Ligand SCK 2 x SCK
Ligand SCU 2 x SCU
Ligand P6G 1 x P6G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 78.935Å b: 110.487Å c: 227.809Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.222
Expression system: Homo sapiens

Quick links

Citations

5 review citations

Acetylcholinesterase: how is structure related to function?
Silman et al. (2008)
4 more

8 mentions without citation

Dynamic Roles of Insect Carboxyl/Cholinesterases in Chemical Adaptation.
Cruse et al. (2023)
7 more