› 6jxg

X-ray diffraction
1.9Å resolution

Crystasl Structure of Beta-glucosidase D2-BGL from Chaetomella Raphigera

Released:
DOI: 10.2210/pdb6jxg/pdb
PDB entry 6jxg coloured by chain, front view.
PDB entry 6jxg coloured by chain, side view.
PDB entry 6jxg coloured by chain, top view.
Source organism: Chaetomella raphigera
Primary publication:
Chaetomella raphigera β-glucosidase D2-BGL has intriguing structural features and a high substrate affinity that renders it an efficient cellulase supplement for lignocellulosic biomass hydrolysis.
Kao MR, Kuo HW, Lee CC, Huang KY, Huang TY, Li CW, Chen CW, Wang AH, Yu SM, Ho TD
OpenAccess logo Biotechnol Biofuels 12 258 (2019)
PMID: 31700541

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-100392 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 722 amino acids
Theoretical weight: 75.78 KDa
Source organism: Chaetomella raphigera
Expression system: Komagataella pastoris
UniProt:
  • Canonical: A0A068FT77 (Residues: 1-722; Coverage: 100%)
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand NAG 3 x NAG
Ligand MAN 1 x MAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL12B2
Spacegroup: P212121
Unit cell:
a: 67.774Å b: 77.661Å c: 123.481Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.145 0.195
Expression system: Komagataella pastoris

Quick links

Citations

2 review citations

Evaluating Enzymatic Productivity-The Missing Link to Enzyme Utility.
Siddiqui et al. (2022)
1 more

3 mentions without citation

Chaetomella raphigera β-glucosidase D2-BGL has intriguing structural features and a high substrate affinity that renders it an efficient cellulase supplement for lignocellulosic biomass hydrolysis.
Kao et al. (2019)
2 more