PDBe 3o9m

X-ray diffraction
2.98Å resolution

Co-crystallization studies of full length recombinant BChE with cocaine offers insights into cocaine detoxification

Released:
Source organism: Homo sapiens
Primary publication:
Cocrystallization studies of full-length recombinant butyrylcholinesterase (BChE) with cocaine.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 434-7 (2011)
PMID: 21505234

Function and Biology Details

Structure analysis Details

Assemblies composition:
homo tetramer (preferred)
homo octamer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 574 amino acids
Theoretical weight: 65.15 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P06276 (Residues: 29-602; Coverage: 100%)
Gene names: BCHE, CHE1
Sequence domains:
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P4212
Unit cell:
a: 150.392Å b: 150.392Å c: 142.448Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.223 0.262
Expression system: Cricetulus griseus