› 2ha6

X-ray diffraction
2.25Å resolution

Crystal structure of mutant S203A of mouse acetylcholinesterase complexed with succinylcholine

Released:
DOI: 10.2210/pdb2ha6/pdb
PDB entry 2ha6 coloured by chain, front view.
PDB entry 2ha6 coloured by chain, side view.
PDB entry 2ha6 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 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: 543 amino acids
Theoretical weight: 59.75 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

3 bound ligands:
Ligand SCK 4 x SCK
Ligand P6G 1 x P6G
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 78.983Å b: 109.825Å c: 227.933Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.177 0.198
Expression system: Homo sapiens

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Citations

5 review citations

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