› 3vik

X-ray diffraction
1.1Å resolution

Crystal structure of beta-glucosidase from termite Neotermes koshunensis in complex with cellobiose

Released:
DOI: 10.2210/pdb3vik/pdb
PDB entry 3vik coloured by chain, front view.
PDB entry 3vik coloured by chain, side view.
PDB entry 3vik coloured by chain, top view.
Source organism: Neotermes koshunensis
Primary publication:
High-resolution structures of Neotermes koshunensis β-glucosidase mutants provide insights into the catalytic mechanism and the synthesis of glucoconjugates.
Jeng WY, Wang NC, Lin CT, Chang WJ, Liu CI, Wang AH
Acta Crystallogr D Biol Crystallogr 68 829-38 (2012)
PMID: 22751668

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 analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-570100 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Beta-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 487 amino acids
Theoretical weight: 55.58 KDa
Source organism: Neotermes koshunensis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8T0W7 (Residues: 21-498; Coverage: 100%)
Gene name: NkBG
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
3 bound ligands:
Ligand EDO 1 x EDO
Ligand NA 1 x NA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL12B2
Spacegroup: C2
Unit cell:
a: 92.965Å b: 68.714Å c: 75.832Å
α: 90° β: 95.73° γ: 90°
R-values:
R R work R free
0.148 0.147 0.168
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Modeled structural basis for the recognition of α2-3-sialyllactose by soluble Klotho.
Wright et al. (2017)
8 more

10 mentions without citation

β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides.
Rohman et al. (2019)
9 more