› 1x39

X-ray diffraction
1.8Å resolution

Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with gluco-phenylimidazole

Released:
DOI: 10.2210/pdb1x39/pdb
PDB entry 1x39 coloured by chain, front view.
PDB entry 1x39 coloured by chain, side view.
PDB entry 1x39 coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Structural rationale for low-nanomolar binding of transition state mimics to a family GH3 beta-D-glucan glucohydrolase from barley.
Hrmova M, Streltsov VA, Smith BJ, Vasella A, Varghese JN, Fincher GB
Biochemistry 44 16529-39 (2005)
PMID: 16342944

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 (4 distinct):
beta-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 602 amino acids
Theoretical weight: 65.05 KDa
Source organism: Hordeum vulgare
UniProt:
  • Canonical: Q9XEI3 (Residues: 26-627; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, XYP, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, XYP, FUC
Carbohydrate polymer
3 bound ligands:
Ligand SO4 2 x SO4
Ligand IDE 1 x IDE
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P43212
Unit cell:
a: 99.991Å b: 99.991Å c: 184.386Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.159 0.185

Quick links

Citations

5 review citations

Mechanistic insights into glycosidase chemistry.
Vocadlo et al. (2008)
4 more

3 mentions without citation

Glycosidase inhibition: assessing mimicry of the transition state.
Gloster et al. (2010)
2 more