› 5ost

X-ray diffraction
2.1Å resolution

Beta-glucosidase from Thermoanaerobacterium xylolyticum GH116 in complex with Gluco-1H-imidazole

Released:
DOI: 10.2210/pdb5ost/pdb
PDB entry 5ost coloured by chain, front view.
PDB entry 5ost coloured by chain, side view.
PDB entry 5ost coloured by chain, top view.
Source organism: Thermoanaerobacterium xylanolyticum LX-11
Primary publication:
Gluco-1 H-imidazole: A New Class of Azole-Type β-Glucosidase Inhibitor.
Schröder SP, Wu L, Artola M, Hansen T, Offen WA, Ferraz MJ, Li KY, Aerts JMFG, van der Marel GA, Codée JDC, Davies GJ, Overkleeft HS
J Am Chem Soc 140 5045-5048 (2018)
PMID: 29601200

Function and Biology Details

Reaction catalysed: 
D-glucosyl-N-acylsphingosine + H(2)O = D-glucose + N-acylsphingosine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123592 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucosylceramidase Chain: A
Molecule details ›
Chain: A
Length: 799 amino acids
Theoretical weight: 91.79 KDa
Source organism: Thermoanaerobacterium xylanolyticum LX-11
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: F6BL85 (Residues: 19-806; Coverage: 98%)
Gene name: Thexy_2211
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand CA 1 x CA
Ligand EDO 8 x EDO
Ligand CL 5 x CL
Ligand AEZ 1 x AEZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21212
Unit cell:
a: 177.617Å b: 54.09Å c: 83.559Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.251
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Chemical Chaperones to Inhibit Endoplasmic Reticulum Stress: Implications in Diseases.
Jeon et al. (2022)
7 other articles

1 mention without citation

Gluco-1 H-imidazole: A New Class of Azole-Type β-Glucosidase Inhibitor.
Schröder et al. (2018)