1ieq

X-ray diffraction
2.7Å resolution

CRYSTAL STRUCTURE OF BARLEY BETA-D-GLUCAN GLUCOHYDROLASE ISOENZYME EXO1

Released:

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:
  • not assigned

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: 605 amino acids
Theoretical weight: 65.48 KDa
Source organism: Hordeum vulgare
UniProt:
  • Canonical: Q9XEI3 (Residues: 26-630; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P43212
Unit cell:
a: 100.951Å b: 100.951Å c: 181.196Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.228