› 6wuy

X-ray diffraction
2.46Å resolution

Crystal Structure of Recombinant Human Acetylcholinesterase In Complex with GA and HI-6

Released:
DOI: 10.2210/pdb6wuy/pdb
PDB entry 6wuy coloured by chain, front view.
PDB entry 6wuy coloured by chain, side view.
PDB entry 6wuy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and Biochemical Insights into the Inhibition of Human Acetylcholinesterase by G-Series Nerve Agents and Subsequent Reactivation by HI-6.
McGuire JR, Bester SM, Guelta MA, Cheung J, Langley C, Winemiller MD, Bae SY, Funk V, Myslinski JM, Pegan SD, Height JJ
Chem Res Toxicol 34 804-816 (2021)
PMID: 33538594

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 (3 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 542 amino acids
Theoretical weight: 59.45 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P22303 (Residues: 33-574; 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
3 bound ligands:
Ligand NAG 1 x NAG
Ligand ELT 2 x ELT
Ligand HI6 2 x HI6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3121
Unit cell:
a: 105.331Å b: 105.331Å c: 324.866Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.179 0.214
Expression system: Homo sapiens

Quick links

Citations

1 citations in other articles

Broad-Spectrum Antidote Discovery by Untangling the Reactivation Mechanism of Nerve-Agent-Inhibited Acetylcholinesterase.
Lindgren et al. (2022)