› 6esy

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reaction catalysed: 
An acylcholine + H(2)O = choline + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138983 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Cholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 529 amino acids
Theoretical weight: 59.66 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: P06276 (Residues: 29-557; Coverage: 92%)
Gene names: BCHE, CHE1
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
3 bound ligands:
Ligand NAG 7 x NAG
Ligand TFX 4 x TFX
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 74.27Å b: 79.25Å c: 228.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.206 0.262
Expression system: Drosophila melanogaster

Quick links

Citations

5 review citations

A Comprehensive Review of Cholinesterase Modeling and Simulation.
De Boer et al. (2021)
4 more

5 mentions without citation

Comparison of the Binding of Reversible Inhibitors to Human Butyrylcholinesterase and Acetylcholinesterase: A Crystallographic, Kinetic and Calorimetric Study.
Rosenberry et al. (2017)
4 more