X-ray diffraction
2.7Å resolution

Crystal structure of the beta-glucosidase Bgl15


Function and Biology Details

Reaction catalysed:
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Beta-glucosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 477 amino acids
Theoretical weight: 52.9 KDa
Source organism: uncultured bacterium
Expression system: Escherichia coli
  • Canonical: A0A5B9BHU3 (Residues: 1-464; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P21
Unit cell:
a: 51.296Å b: 93.353Å c: 94.057Å
α: 90° β: 104.2° γ: 90°
R R work R free
0.22 0.219 0.254
Expression system: Escherichia coli