PDBe 1ghs

X-ray diffraction
2.3Å resolution

THE THREE-DIMENSIONAL STRUCTURES OF TWO PLANT BETA-GLUCAN ENDOHYDROLASES WITH DISTINCT SUBSTRATE SPECIFICITIES

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucan endo-1,3-beta-glucosidase GII Chains: A, B
Molecule details ›
Chains: A, B
Length: 306 amino acids
Theoretical weight: 32.38 KDa
Source organism: Hordeum vulgare
Expression system: Not provided
UniProt:
  • Canonical: P15737 (Residues: 29-334; Coverage: 100%)
Sequence domains: Glycosyl hydrolases family 17
Structure domains: Glycosidases

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 86.9Å b: 86.9Å c: 156Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.179 not available
Expression system: Not provided