› 2z1s

X-ray diffraction
2.46Å resolution

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149651 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Beta-glucosidase B Chain: A
Molecule details ›
Chain: A
Length: 454 amino acids
Theoretical weight: 52.55 KDa
Source organism: Paenibacillus polymyxa
Expression system: Escherichia coli
UniProt:
  • Canonical: P22505 (Residues: 2-448; Coverage: 100%)
Gene name: bglB
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P212121
Unit cell:
a: 71.324Å b: 75.283Å c: 88.794Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.215 0.272
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Biotransformation of ginsenosides by hydrolyzing the sugar moieties of ginsenosides using microbial glycosidases.
Park et al. (2010)
4 more

6 mentions without citation

Structures of β-klotho reveal a 'zip code'-like mechanism for endocrine FGF signalling.
Lee et al. (2018)
5 more