› 7ait

X-ray diffraction
2.1Å resolution

Crystal structure of Torpedo Californica acetylcholinesterase in complex with 7-[(3-Chloro-6,7,10,11-tetrahydro-9-methyl-7,11-methanocycloocta[b]quinolin-12-yl)amino]-N-(4-hydroxy-3-methoxybenzyl)heptanamide

Released:
DOI: 10.2210/pdb7ait/pdb
PDB entry 7ait coloured by chain, front view.
PDB entry 7ait coloured by chain, side view.
PDB entry 7ait coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Discovery of a Potent Dual Inhibitor of Acetylcholinesterase and Butyrylcholinesterase with Antioxidant Activity that Alleviates Alzheimer-like Pathology in Old APP/PS1 Mice.
Viayna E, Coquelle N, Cieslikiewicz-Bouet M, Cisternas P, Oliva CA, Sánchez-López E, Ettcheto M, Bartolini M, De Simone A, Ricchini M, Rendina M, Pons M, Firuzi O, Pérez B, Saso L, Andrisano V, Nachon F, Brazzolotto X, García ML, Camins A, Silman I, Jean L, Inestrosa NC, Colletier JP, Renard PY, Muñoz-Torrero D
J Med Chem 64 812-839 (2021)
PMID: 33356266

Function and Biology Details

Reaction catalysed: 
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
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: 586 amino acids
Theoretical weight: 65.97 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 1-586; Coverage: 100%)
Gene name: ache
Sequence domains: Carboxylesterase family

Ligands and Environments

1 bound ligand:
Ligand 8UK 2 x 8UK
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: P212121
Unit cell:
a: 92.42Å b: 106.85Å c: 151.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.227

Quick links

Citations

2 review citations

Tacrine-Based Hybrids: Past, Present, and Future.
Bubley et al. (2023)
1 more