› 3f5j

X-ray diffraction
1.95Å resolution

Semi-active E176Q mutant of rice BGlu1, a plant exoglucanase/beta-glucosidase

Released:
DOI: 10.2210/pdb3f5j/pdb
PDB entry 3f5j coloured by chain, front view.
PDB entry 3f5j coloured by chain, side view.
PDB entry 3f5j coloured by chain, top view.
Source organism: Oryza sativa Japonica Group
Primary publication:
The structural basis of oligosaccharide binding by rice BGlu1 beta-glucosidase.
Chuenchor W, Pengthaisong S, Robinson RC, Yuvaniyama J, Svasti J, Cairns JR
J Struct Biol 173 169-79 (2011)
PMID: 20884352

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-181114 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Beta-glucosidase 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 481 amino acids
Theoretical weight: 54.73 KDa
Source organism: Oryza sativa Japonica Group
Expression system: Escherichia coli
UniProt:
  • Canonical: Q75I93 (Residues: 29-504; Coverage: 100%)
Gene names: BGLU1, BGLU7, LOC_Os03g49600, OSJNBa0004L11.16, Os03g0703000
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
3 bound ligands:
Ligand ZN 1 x ZN
Ligand SO4 2 x SO4
Ligand MES 2 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P212121
Unit cell:
a: 79.731Å b: 100.843Å c: 127.472Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.214
Expression system: Escherichia coli

Quick links

Citations

2 review citations

β-Glucosidases: Multitasking, moonlighting or simply misunderstood?
Ketudat Cairns et al. (2015)
1 more

5 mentions without citation

Ligand-binding specificity and promiscuity of the main lignocellulolytic enzyme families as revealed by active-site architecture analysis.
Tian et al. (2016)
4 more