› 1vxo

X-ray diffraction
2.4Å resolution

METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED) OBTAINED BY REACTION WITH O-ETHYL-S-[2-[BIS(1-METHYLETHYL)AMINO]ETHYL] METHYLPHOSPHONOTHIOATE (VX)

Released:
DOI: 10.2210/pdb1vxo/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1vxo coloured by chain, front view.
PDB entry 1vxo coloured by chain, side view.
PDB entry 1vxo coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Reaction Products of Acetylcholinesterase and VX Reveal a Mobile Histidine in the Catalytic Triad
Millard CB, Koellner G, Ordentlich A, Shafferman A, Silman I, Sussman JL
J. Am. Chem. Soc. 121 9883-9884 (1999)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137374 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 537 amino acids
Theoretical weight: 60.74 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 22-558; Coverage: 95%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand NAG 2 x NAG
Ligand VXA 1 x VXA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P3121
Unit cell:
a: 112.509Å b: 112.509Å c: 137.955Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.194 0.234

Quick links

Citations

1 mention without citation

Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics.
Xu et al. (2008)