› 1ax9

X-ray diffraction
2.8Å resolution

ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, LAUE DATA

Released:
DOI: 10.2210/pdb1ax9/pdb
PDB entry 1ax9 coloured by chain, front view.
PDB entry 1ax9 coloured by chain, side view.
PDB entry 1ax9 coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Static Laue diffraction studies on acetylcholinesterase.
Ravelli RB, Raves ML, Ren Z, Bourgeois D, Roth M, Kroon J, Silman I, Sussman JL
Acta Crystallogr D Biol Crystallogr 54 1359-66 (1998)
PMID: 10089512

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-137375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 537 amino acids
Theoretical weight: 60.74 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 22-558; Coverage: 95%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand EDR 1 x EDR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID09
Spacegroup: P3121
Unit cell:
a: 113Å b: 113Å c: 136.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 not available 0.268

Quick links

Citations

1 review citation

Molecular interactions of cholinesterases inhibitors using in silico methods: current status and future prospects.
Khan MT. (2009)
15 other articles

6 mentions without citation

Molecular dynamics simulations: advances and applications.
Hospital et al. (2015)
5 more