PDBe 1aq0

X-ray diffraction
2Å resolution

BARLEY 1,3-1,4-BETA-GLUCANASE IN MONOCLINIC SPACE GROUP

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lichenase-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 306 amino acids
Theoretical weight: 32.14 KDa
Source organism: Hordeum vulgare
UniProt:
  • Canonical: P12257 (Residues: 7-312; Coverage: 100%)
Sequence domains: Glycosyl hydrolases family 17
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P21
Unit cell:
a: 49.58Å b: 82.99Å c: 77.56Å
α: 90° β: 104.36° γ: 90°
R-values:
R R work R free
0.17 0.17 0.213