› 2jfe

X-ray diffraction
2.7Å resolution

The crystal structure of human cytosolic beta-glucosidase

Released:
DOI: 10.2210/pdb2jfe/pdb
PDB entry 2jfe coloured by chain, front view.
PDB entry 2jfe coloured by chain, side view.
PDB entry 2jfe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of human cytosolic beta-glucosidase unravels the substrate aglycone specificity of a family 1 glycoside hydrolase.
Tribolo S, Berrin JG, Kroon PA, Czjzek M, Juge N
J Mol Biol 370 964-75 (2007)
PMID: 17555766

Function and Biology Details

Reactions catalysed: 
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
D-glucosyl-N-acylsphingosine + H(2)O = D-glucose + N-acylsphingosine
D-galactosyl-N-acylsphingosine + H(2)O = D-galactose + N-acylsphingosine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190531 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Cytosolic beta-glucosidase Chain: X
Molecule details ›
Chain: X
Length: 469 amino acids
Theoretical weight: 53.74 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q9H227 (Residues: 1-469; Coverage: 100%)
Gene names: CBG, CBGL1, GBA3
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P3121
Unit cell:
a: 90.479Å b: 90.479Å c: 127.925Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.197 0.28
Expression system: Komagataella pastoris

Quick links

Citations

4 review citations

β-Glucosidases.
Ketudat Cairns et al. (2010)
3 more

3 mentions without citation

Aglycone specificity of Thermotoga neapolitana β-glucosidase 1A modified by mutagenesis, leading to increased catalytic efficiency in quercetin-3-glucoside hydrolysis.
Khan et al. (2011)
2 more