4hz6

X-ray diffraction
1.4Å resolution

crystal structure of BglB

Released:
Source organism: uncultured bacterium
Primary publication:
Structural insights into the substrate recognition properties of beta-glucosidase.
Biochem Biophys Res Commun 391 1131-5 (2010)
PMID: 20005197

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170935 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 444 amino acids
Theoretical weight: 50.29 KDa
Source organism: uncultured bacterium
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0GMU3 (Residues: 39-482; Coverage: 92%)
Gene name: bglA
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6C1
Spacegroup: P212121
Unit cell:
a: 70.697Å b: 71.143Å c: 87.373Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.138 0.179
Expression system: Escherichia coli