PDBe 1ex1

X-ray diffraction
2.2Å resolution

BETA-D-GLUCAN EXOHYDROLASE FROM BARLEY

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
Macromolecule:
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


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE M18X
Spacegroup: P43212
Unit cell:
a: 102.09Å b: 102.09Å c: 184.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 0.202