› 4r27

X-ray diffraction
2.03Å resolution

Crystal structure of beta-glycosidase BGL167

Released:
DOI: 10.2210/pdb4r27/pdb
PDB entry 4r27 coloured by chain, front view.
PDB entry 4r27 coloured by chain, side view.
PDB entry 4r27 coloured by chain, top view.
Source organism: Microbacterium sp. Gsoil167
Primary publication:
Rational design of a β-glycosidase with high regiospecificity for triterpenoid tailoring.
Park SJ, Choi JM, Kyeong HH, Kim SG, Kim HS
Chembiochem 16 854-60 (2015)
PMID: 25703680

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125744 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycoside hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 434 amino acids
Theoretical weight: 47.81 KDa
Source organism: Microbacterium sp. Gsoil167
Expression system: Escherichia coli
UniProt:
  • Canonical: L0ELG0 (Residues: 5-425; Coverage: 99%)
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: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P21
Unit cell:
a: 48.498Å b: 146.94Å c: 53.041Å
α: 90° β: 101.99° γ: 90°
R-values:
R R work R free
0.196 0.191 0.239
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biocatalytic strategies for the production of ginsenosides using glycosidase: current state and perspectives.
Li et al. (2020)
1 more

2 mentions without citation

Production of Gypenoside XVII from Ginsenoside Rb1 by Enzymatic Transformation and Their Anti-Inflammatory Activity In Vitro and In Vivo.
Zhou et al. (2023)
1 more