› 6md6

X-ray diffraction
1.68Å resolution

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195007 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
beta-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 609 amino acids
Theoretical weight: 65.89 KDa
Source organism: Hordeum vulgare subsp. vulgare
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q9XEI3 (Residues: 25-630; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: U2A, BGC
Ligand U2A 1 x U2A
Ligand BGC 1 x BGC
4 bound ligands:
Ligand NAG 3 x NAG
Ligand GOL 10 x GOL
Ligand SO4 2 x SO4
Ligand 1PE 6 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P43212
Unit cell:
a: 100.311Å b: 100.311Å c: 182.153Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 0.132 0.159
Expression system: Komagataella pastoris

Quick links

Citations

2 review citations

Research progress and the biotechnological applications of multienzyme complex.
Jiang et al. (2021)
1 more

2 mentions without citation

Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site.
Streltsov et al. (2019)
1 more