› 2whp

X-ray diffraction
2.2Å resolution

Crystal structure of acetylcholinesterase, phosphonylated by sarin and in complex with HI-6

Released:
DOI: 10.2210/pdb2whp/pdb
PDB entry 2whp coloured by chain, front view.
PDB entry 2whp coloured by chain, side view.
PDB entry 2whp coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structure of HI-6*sarin-acetylcholinesterase determined by X-ray crystallography and molecular dynamics simulation: reactivator mechanism and design.
Ekström F, Hörnberg A, Artursson E, Hammarström LG, Schneider G, Pang YP
OpenAccess logo PLoS One 4 e5957 (2009)
PMID: 19536291

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-149440 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 548 amino acids
Theoretical weight: 60.35 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 32-576; Coverage: 94%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase
Acetylcholinesterase Chain: B
Molecule details ›
Chain: B
Length: 548 amino acids
Theoretical weight: 60.34 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 32-576; Coverage: 94%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

5 bound ligands:
Ligand NAG 3 x NAG
Ligand HI6 2 x HI6
Ligand CO3 1 x CO3
Ligand PEG 1 x PEG
Ligand P6G 1 x P6G
1 modified residue:
Ligand SGB 2 x SGB

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P212121
Unit cell:
a: 79.26Å b: 112.15Å c: 226.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.175 0.21
Expression system: Homo sapiens

Quick links

Citations

3 review citations

The value of novel oximes for treatment of poisoning by organophosphorus compounds.
Worek et al. (2013)
2 more

10 mentions without citation

Limitations in current acetylcholinesterase structure-based design of oxime antidotes for organophosphate poisoning.
Kovalevsky et al. (2016)
9 more