› 8aev

X-ray diffraction
2.89Å resolution

Human acetylcholinesterase in complex with N,N,N-trimethyl-2-oxo-2-(2-(pyridin-2-ylmethylene)hydrazineyl)ethan-1-aminium

Released:
DOI: 10.2210/pdb8aev/pdb
PDB entry 8aev coloured by chain, front view.
PDB entry 8aev coloured by chain, side view.
PDB entry 8aev coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Grid-Type Quaternary Metallosupramolecular Compounds Inhibit Human Cholinesterases through Dynamic Multivalent Interactions.
Nachon F, Brazzolotto X, Dias J, Courageux C, Drożdż W, Cao XY, Stefankiewicz AR, Lehn JM
Chembiochem 23 e202200456 (2022)
PMID: 36193860

Function and Biology Details

Reaction catalysed: 
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149584 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 543 amino acids
Theoretical weight: 59.64 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P22303 (Residues: 32-574; Coverage: 93%)
Gene name: ACHE
Sequence domains: Carboxylesterase family

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GAL, SIA
Carbohydrate polymer
5 bound ligands:
Ligand LWU 1 x LWU
Ligand SO4 16 x SO4
Ligand CL 31 x CL
Ligand ZN 5 x ZN
Ligand MG 14 x MG
1 modified residue:
Ligand TIS 2 x TIS

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P61
Unit cell:
a: 211.833Å b: 211.833Å c: 116.634Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.184 0.207
Expression system: Cricetulus griseus

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