› 7qb4

X-ray diffraction
2.5Å resolution

Mus Musculus Acetylcholinesterase in complex with 7-[(1-benzylpiperidin-3-yl)methoxy]-3,4-dimethyl-2H-chromen-2-one

Released:
DOI: 10.2210/pdb7qb4/pdb
PDB entry 7qb4 coloured by chain, front view.
PDB entry 7qb4 coloured by chain, side view.
PDB entry 7qb4 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Dual Reversible Coumarin Inhibitors Mutually Bound to Monoamine Oxidase B and Acetylcholinesterase Crystal Structures.
Ekström F, Gottinger A, Forsgren N, Catto M, Iacovino LG, Pisani L, Binda C
ACS Med Chem Lett 13 499-506 (2022)
PMID: 35300078

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-149441 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 543 amino acids
Theoretical weight: 59.76 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 32-574; Coverage: 93%)
Gene name: Ache
Sequence domains: Carboxylesterase family

Ligands and Environments

6 bound ligands:
Ligand NAG 3 x NAG
Ligand AJ9 2 x AJ9
Ligand PG0 15 x PG0
Ligand EDO 3 x EDO
Ligand TOE 1 x TOE
Ligand 9YU 1 x 9YU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX IV BEAMLINE BioMAX
Spacegroup: P212121
Unit cell:
a: 79.406Å b: 111.048Å c: 227.092Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.184 0.217
Expression system: Homo sapiens

Quick links

Citations

1 review citation

A twenty-year journey exploring coumarin-based derivatives as bioactive molecules.
Pisani et al. (2022)
3 other articles

1 mention without citation

Dual Reversible Coumarin Inhibitors Mutually Bound to Monoamine Oxidase B and Acetylcholinesterase Crystal Structures.
Ekström et al. (2022)