› 6g1v

X-ray diffraction
1.82Å resolution

Crystal structure of Torpedo Californica acetylcholinesterase in complex with 12-Amino-3-chloro-6,7,10,11-tetrahydro-5,9-dimethyl-7,11-methanocycloocta[b]quinolin-5-ium

Released:
DOI: 10.2210/pdb6g1v/pdb
PDB entry 6g1v coloured by chain, front view.
PDB entry 6g1v coloured by chain, side view.
PDB entry 6g1v coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Increasing Polarity in Tacrine and Huprine Derivatives: Potent Anticholinesterase Agents for the Treatment of Myasthenia Gravis.
Galdeano C, Coquelle N, Cieslikiewicz-Bouet M, Bartolini M, Pérez B, Clos MV, Silman I, Jean L, Colletier JP, Renard PY, Muñoz-Torrero D
Molecules 23 (2018)
PMID: 29534488

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 565 amino acids
Theoretical weight: 63.76 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 22-586; Coverage: 100%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

4 bound ligands:
Ligand NAG 6 x NAG
Ligand E1N 2 x E1N
Ligand CL 4 x CL
Ligand PEG 3 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: P212121
Unit cell:
a: 91.74Å b: 106.44Å c: 150.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.188 0.217

Quick links

Citations

1 review citation

Effects of Natural Products on Neuromuscular Junction.
Akkol et al. (2022)
8 other articles

1 mention without citation

Structural Isomerism and Enhanced Lipophilicity of Pyrithione Ligands of Organoruthenium(II) Complexes Increase Inhibition on AChE and BuChE.
Kladnik et al. (2020)