› 1oin

X-ray diffraction
2.15Å 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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-555165 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucosidase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 468 amino acids
Theoretical weight: 53.94 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q08638 (Residues: 2-446; Coverage: 100%)
Gene name: bglA
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

1 bound ligand:
Ligand G2F 2 x G2F
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 94.91Å b: 94.98Å c: 113.928Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.256
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

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

5 mentions without citation

Biochemical and structural characterization of a thermostable β-glucosidase from Halothermothrix orenii for galacto-oligosaccharide synthesis.
Hassan et al. (2015)
4 more