› 1c2o

X-ray diffraction
4.2Å resolution

ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE

Released:
DOI: 10.2210/pdb1c2o/pdb
PDB entry 1c2o coloured by chain, front view.
PDB entry 1c2o coloured by chain, side view.
PDB entry 1c2o coloured by chain, top view.
Source organism: Electrophorus electricus
Primary publication:
Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallography.
Bourne Y, Grassi J, Bougis PE, Marchot P
J Biol Chem 274 30370-6 (1999)
PMID: 10521413

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
Macromolecule:
Acetylcholinesterase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 539 amino acids
Theoretical weight: 59.29 KDa
Source organism: Electrophorus electricus
UniProt:
  • Canonical: P21836 (Residues: 36-574; Coverage: 93%)
Gene name: Ache
Sequence domains: Carboxylesterase family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 211.16Å b: 129.75Å c: 195.42Å
α: 90° β: 103.2° γ: 90°
R-values:
R R work R free
0.375 0.375 0.385

Quick links

Citations

5 review citations

Novel multitarget-directed tacrine derivatives as potential candidates for the treatment of Alzheimer's disease.
Wu et al. (2017)
4 more

36 mentions without citation

Hot Spots for Protein Partnerships at the Surface of Cholinesterases and Related α/β Hydrolase Fold Proteins or Domains-A Structural Perspective.
Bourne et al. (2017)
35 more