› 4aqd

X-ray diffraction
2.5Å resolution

Crystal structure of fully glycosylated human butyrylcholinesterase

Released:
DOI: 10.2210/pdb4aqd/pdb
PDB entry 4aqd coloured by chain, front view.
PDB entry 4aqd coloured by chain, side view.
PDB entry 4aqd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human butyrylcholinesterase produced in insect cells: huprine-based affinity purification and crystal structure.
Brazzolotto X, Wandhammer M, Ronco C, Trovaslet M, Jean L, Lockridge O, Renard PY, Nachon F
FEBS J 279 2905-16 (2012)
PMID: 22726956

Function and Biology Details

Reaction catalysed: 
An acylcholine + H(2)O = choline + a carboxylate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
monomeric
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: 531 amino acids
Theoretical weight: 59.9 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: P06276 (Residues: 27-557; 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
Carbohydrate polymer : NEW Components: NAG, FUL
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
8 bound ligands:
Ligand BAL 2 x BAL
Ligand NAG 6 x NAG
Ligand PG4 2 x PG4
Ligand EDO 19 x EDO
Ligand UNX 10 x UNX
Ligand CL 7 x CL
Ligand GLY 2 x GLY
Ligand PEG 2 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 72.75Å b: 79.26Å c: 227.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.163 0.232
Expression system: Drosophila melanogaster

Quick links

Citations

8 review citations

Review of human butyrylcholinesterase structure, function, genetic variants, history of use in the clinic, and potential therapeutic uses.
Lockridge O. (2015)
7 more

10 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)
9 more