› 2v97

X-ray diffraction
2.4Å resolution

Structure of the unphotolysed complex of TcAChE with 1-(2- nitrophenyl)-2,2,2-trifluoroethyl-arsenocholine after a 9 seconds annealing to room temperature

Released:
DOI: 10.2210/pdb2v97/pdb
PDB entry 2v97 coloured by chain, front view.
PDB entry 2v97 coloured by chain, side view.
PDB entry 2v97 coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Use of a 'caged' analogue to study the traffic of choline within acetylcholinesterase by kinetic crystallography.
Colletier JP, Royant A, Specht A, Sanson B, Nachon F, Masson P, Zaccai G, Sussman JL, Goeldner M, Silman I, Bourgeois D, Weik M
Acta Crystallogr D Biol Crystallogr 63 1115-28 (2007)
PMID: 18007027

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
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

3 bound ligands:
Ligand CL 1 x CL
Ligand CFQ 4 x CFQ
Ligand NAG 4 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 91.2Å b: 104.46Å c: 148.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.272

Quick links

Citations

4 review citations

Resurrection and Reactivation of Acetylcholinesterase and Butyrylcholinesterase.
Franjesevic et al. (2019)
3 more