› 5k5e

X-ray diffraction
2.8Å resolution

Discovery and Structure-Activity Relationships of a Highly Selective Butyrylcholinesterase Inhibitor by Structure-Based Virtual Screening

Released:
DOI: 10.2210/pdb5k5e/pdb
PDB entry 5k5e coloured by chain, front view.
PDB entry 5k5e coloured by chain, side view.
PDB entry 5k5e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery and Structure-Activity Relationships of a Highly Selective Butyrylcholinesterase Inhibitor by Structure-Based Virtual Screening.
Dighe SN, Deora GS, De la Mora E, Nachon F, Chan S, Parat MO, Brazzolotto X, Ross BP
J Med Chem 59 7683-9 (2016)
PMID: 27405689

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 (2 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
Carbohydrate polymer
4 bound ligands:
Ligand NAG 10 x NAG
Ligand 6QS 2 x 6QS
Ligand EDO 3 x EDO
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 75.81Å b: 80.07Å c: 230.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.202
Expression system: Drosophila melanogaster

Quick links

Citations

8 review citations

Recent progress in the identification of selective butyrylcholinesterase inhibitors for Alzheimer's disease.
Li et al. (2017)
7 more

8 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)
7 more