X-ray diffraction
2.7Å resolution

Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with gluco-phenylimidazole


Function and Biology Details

Reaction catalysed:
Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Beta-D-glucan exohydrolase isoenzyme ExoI Chain: A
Molecule details ›
Chain: A
Length: 602 amino acids
Theoretical weight: 65.05 KDa
Source organism: Hordeum vulgare
  • Canonical: Q9XEI3 (Residues: 26-627; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, MAN, FUC
Carbohydrate polymer : NEW Components: NAG, FUC, BMA
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P43212
Unit cell:
a: 100.693Å b: 100.693Å c: 182.676Å
α: 90° β: 90° γ: 90°
R R work R free
0.21 0.21 0.273