› 1ex1

X-ray diffraction
2.2Å resolution

BETA-D-GLUCAN EXOHYDROLASE FROM BARLEY

Released:
DOI: 10.2210/pdb1ex1/pdb
PDB entry 1ex1 coloured by chain, front view.
PDB entry 1ex1 coloured by chain, side view.
PDB entry 1ex1 coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase.
Varghese JN, Hrmova M, Fincher GB
Structure 7 179-90 (1999)
PMID: 10368285

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 (2 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, MAN, FCA
Carbohydrate polymer
2 bound ligands:
Ligand NAG 1 x NAG
Ligand GLC 1 x GLC
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

Quick links

Citations

16 review citations

Microbial beta-glucosidases: cloning, properties, and applications.
Bhatia et al. (2002)
15 more

24 mentions without citation

Enzymatic deconstruction of xylan for biofuel production.
Dodd et al. (2009)
23 more