› 1np2

X-ray diffraction
2.4Å resolution

Crystal structure of thermostable beta-glycosidase from thermophilic eubacterium Thermus nonproteolyticus HG102

Released:
DOI: 10.2210/pdb1np2/pdb
PDB entry 1np2 coloured by chain, front view.
PDB entry 1np2 coloured by chain, side view.
PDB entry 1np2 coloured by chain, top view.
Source organism: Thermus nonproteolyticus
Primary publication:
Structural basis for thermostability of beta-glycosidase from the thermophilic eubacterium Thermus nonproteolyticus HG102.
Wang X, He X, Yang S, An X, Chang W, Liang D
J Bacteriol 185 4248-55 (2003)
PMID: 12837801

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 436 amino acids
Theoretical weight: 49.06 KDa
Source organism: Thermus nonproteolyticus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9L794 (Residues: 1-436; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: P212121
Unit cell:
a: 66.7Å b: 94.755Å c: 176.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.23 0.272
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Thermostable enzymes as biocatalysts in the biofuel industry.
Yeoman et al. (2010)
12 other articles

5 mentions without citation

High resolution crystal structure of human β-glucuronidase reveals structural basis of lysosome targeting.
Hassan et al. (2013)
4 more