PDBe 4aqd

X-ray diffraction
2.5Å resolution

Crystal structure of fully glycosylated human butyrylcholinesterase

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
monomeric
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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: Rossmann fold

Ligands and Environments

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