› 1ghs

X-ray diffraction
2.3Å resolution

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

Released:
DOI: 10.2210/pdb1ghs/pdb
PDB entry 1ghs coloured by chain, front view.
PDB entry 1ghs coloured by chain, side view.
PDB entry 1ghs coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities.
Varghese JN, Garrett TP, Colman PM, Chen L, Høj PB, Fincher GB
Proc Natl Acad Sci U S A 91 2785-9 (1994)
PMID: 8146192

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147476 (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

Quick links

Citations

8 review citations

Structures and mechanisms of glycosyl hydrolases.
Davies et al. (1995)
7 more

6 mentions without citation

Selection on Glycine beta-1,3-endoglucanase genes differentially inhibited by a Phytophthora glucanase inhibitor protein.
Bishop et al. (2005)
5 more