PDBe 2pm8

X-ray diffraction
2.8Å resolution

Crystal structure of recombinant full length human butyrylcholinesterase

Released:
Source organism: Homo sapiens
Primary publication:
Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 723-7 (2007)
PMID: 17768338

Function and Biology Details

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 574 amino acids
Theoretical weight: 65.21 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


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P4212
Unit cell:
a: 150.803Å b: 150.803Å c: 142.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.222 0.292
Expression system: Cricetulus griseus