X-ray diffraction
1.9Å resolution

Crystal Structure of the Covalent Intermediate of Human Cytosolic beta-Glucosidase

Source organism: Homo sapiens
Primary publication:
Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase.
Biochem. Biophys. Res. Commun. 374 549-52 (2008)
PMID: 18662675

Function and Biology Details

Reaction catalysed:
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Cytosolic beta-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 469 amino acids
Theoretical weight: 53.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q9H227 (Residues: 1-469; Coverage: 100%)
Gene names: CBG, CBGL1, GBA3
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 66.12Å b: 82.529Å c: 91.673Å
α: 90° β: 90° γ: 90°
R R work R free
0.192 0.191 0.226
Expression system: Escherichia coli