› 3lii

X-ray diffraction
3.2Å resolution

Recombinant human acetylcholinesterase

Released:
DOI: 10.2210/pdb3lii/pdb
PDB entry 3lii coloured by chain, front view.
PDB entry 3lii coloured by chain, side view.
PDB entry 3lii coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Acetylcholinesterase: from 3D structure to function.
Dvir H, Silman I, Harel M, Rosenberry TL, Sussman JL
Chem Biol Interact 187 10-22 (2010)
PMID: 20138030

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-149584 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 540 amino acids
Theoretical weight: 59.23 KDa
Source organism: Homo sapiens
Expression system: Drosophila
UniProt:
  • Canonical: P22303 (Residues: 35-574; Coverage: 93%)
Gene name: ACHE
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand SO4 9 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P61
Unit cell:
a: 210.9Å b: 210.9Å c: 115.27Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.176 0.22
Expression system: Drosophila

Quick links

Citations

31 review citations

Naturally Occurring Acetylcholinesterase Inhibitors and Their Potential Use for Alzheimer's Disease Therapy.
Dos Santos et al. (2018)
30 more

23 mentions without citation

Cryo-electron microscopy of cholinesterases, present and future.
Leung et al. (2021)
22 more