› 6o69

X-ray diffraction
2.08Å resolution

Crystal Structure of Double Mutant L380R/F535K of Human Acetylcholinesterase

Released:
DOI: 10.2210/pdb6o69/pdb
PDB entry 6o69 coloured by chain, front view.
PDB entry 6o69 coloured by chain, side view.
PDB entry 6o69 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structural and biochemical impacts of monomerizing human acetylcholinesterase.
Bester SM, Adipietro KA, Funk VL, Myslinski JM, Keul ND, Cheung J, Wilder PT, Wood ZA, Weber DJ, Height JJ, Pegan SD
Protein Sci 28 1106-1114 (2019)
PMID: 30993792

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149582 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 542 amino acids
Theoretical weight: 59.47 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P22303 (Residues: 33-574; Coverage: 93%)
Gene name: ACHE
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P6522
Unit cell:
a: 115.783Å b: 115.783Å c: 191.859Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.186 0.222
Expression system: Homo sapiens

Quick links

Citations

3 citation in other articles

Reactivation of VX-Inhibited Human Acetylcholinesterase by Deprotonated Pralidoxime. A Complementary Quantum Mechanical Study.
da Silva et al. (2020)
2 more

2 mentions without citation

Integrated meta-analysis, network pharmacology, and molecular docking to investigate the efficacy and potential pharmacological mechanism of Kai-Xin-San on Alzheimer's disease.
Yi et al. (2020)
1 more