› 5dtj

X-ray diffraction
2.71Å resolution

Crystal Structure of dfp-inhibited mouse acetylcholinesterase in complex with the reactivator SP-134

Released:
DOI: 10.2210/pdb5dtj/pdb
PDB entry 5dtj coloured by chain, front view.
PDB entry 5dtj coloured by chain, side view.
PDB entry 5dtj coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Discovery of New Classes of Compounds that Reactivate Acetylcholinesterase Inhibited by Organophosphates.
Katz FS, Pecic S, Tran TH, Trakht I, Schneider L, Zhu Z, Ton-That L, Luzac M, Zlatanic V, Damera S, Macdonald J, Landry DW, Tong L, Stojanovic MN
Chembiochem 16 2205-2215 (2015)
PMID: 26350723

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-149441 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 545 amino acids
Theoretical weight: 60.13 KDa
Source organism: Mus musculus
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P21836 (Residues: 32-573; Coverage: 93%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand 5G8 4 x 5G8
1 modified residue:
Ligand MIS 2 x MIS

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 79.487Å b: 113.367Å c: 227.117Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.221
Expression system: Trichoplusia ni

Quick links

Citations

13 review citations

Cholinesterase reactivators and bioscavengers for pre- and post-exposure treatments of organophosphorus poisoning.
Masson et al. (2017)
12 more