› 6jfp

X-ray diffraction
2.7Å resolution

Crystal structure of the beta-glucosidase Bgl15

Released:
DOI: 10.2210/pdb6jfp/pdb
PDB entry 6jfp coloured by chain, front view.
PDB entry 6jfp coloured by chain, side view.
PDB entry 6jfp coloured by chain, top view.
Source organism: uncultured bacterium
Primary publication:
Engineering of β-Glucosidase Bgl15 with Simultaneously Enhanced Glucose Tolerance and Thermostability To Improve Its Performance in High-Solid Cellulose Hydrolysis.
Cao L, Chen R, Huang X, Li S, Zhang S, Yang X, Qin Z, Kong W, Xie W, Liu Y
J Agric Food Chem 68 5391-5401 (2020)
PMID: 32338906

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-105330 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: A0A5B9BHU3 (Residues: 1-464; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 1

Ligands and Environments

1 bound ligand:
Ligand BGC 1 x BGC
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-values:
R R work R free
0.22 0.219 0.254
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Fungal cellulases: protein engineering and post-translational modifications.
Zhang et al. (2022)
1 more