› 6fqn

X-ray diffraction
2.3Å resolution

Carbamylated T. californica acetylcholineterase bound to uncharged hybrid reactivator 2

Released:
DOI: 10.2210/pdb6fqn/pdb
PDB entry 6fqn coloured by chain, front view.
PDB entry 6fqn coloured by chain, side view.
PDB entry 6fqn coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Structure-Based Optimization of Nonquaternary Reactivators of Acetylcholinesterase Inhibited by Organophosphorus Nerve Agents.
Santoni G, de Sousa J, de la Mora E, Dias J, Jean L, Sussman JL, Silman I, Renard PY, Brown RCD, Weik M, Baati R, Nachon F
J Med Chem 61 7630-7639 (2018)
PMID: 30125110

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-137375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 532 amino acids
Theoretical weight: 60.28 KDa
Source organism: Tetronarce californica
Expression system: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 25-556; Coverage: 94%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

5 bound ligands:
Ligand E2W 1 x E2W
Ligand NAG 3 x NAG
Ligand EDO 2 x EDO
Ligand CL 6 x CL
Ligand P6G 1 x P6G
1 modified residue:
Ligand BXT 1 x BXT

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P3121
Unit cell:
a: 113.43Å b: 113.43Å c: 137.57Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.205 0.234
Expression system: Tetronarce californica

Quick links

Citations

3 review citations

Resurrection and Reactivation of Acetylcholinesterase and Butyrylcholinesterase.
Franjesevic et al. (2019)
2 more

1 mention without citation

Structural and dynamic effects of paraoxon binding to human acetylcholinesterase by X-ray crystallography and inelastic neutron scattering.
Gerlits et al. (2022)