PDBe 3scn

X-ray diffraction
2.2Å resolution

Crystal Structure of Rice BGlu1 E386G Mutant

Released:
Source organism: Oryza sativa Japonica Group
Entry authors: Pengthaisong S, Withers SG, Kuaprasert B, Ketudat Cairns JR

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucosidase 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 481 amino acids
Theoretical weight: 54.66 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

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 79.382Å b: 100.828Å c: 127.415Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.195 0.24
Expression system: Escherichia coli