› 1ieq

X-ray diffraction
2.7Å resolution

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

Released:
DOI: 10.2210/pdb1ieq/pdb
PDB entry 1ieq coloured by chain, front view.
PDB entry 1ieq coloured by chain, side view.
PDB entry 1ieq coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant beta-D-glucan glucohydrolase.
Hrmova M, Varghese JN, De Gori R, Smith BJ, Driguez H, Fincher GB
Structure 9 1005-16 (2001)
PMID: 11709165

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195007 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
beta-glucosidase 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
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
Carbohydrate polymer
1 bound ligand:
Ligand BGC 1 x BGC
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

Quick links

Citations

5 review citations

β-Glucosidases.
Ketudat Cairns et al. (2010)
4 more

5 mentions without citation

Functional and Structural Analysis of a β-Glucosidase Involved in β-1,2-Glucan Metabolism in Listeria innocua.
Nakajima et al. (2016)
4 more