› 2vrj

X-ray diffraction
1.9Å resolution

Beta-glucosidase from Thermotoga maritima in complex with N-octyl-5- deoxy-6-oxa-N-(thio)carbamoylcalystegine

Released:
DOI: 10.2210/pdb2vrj/pdb
PDB entry 2vrj coloured by chain, front view.
PDB entry 2vrj coloured by chain, side view.
PDB entry 2vrj coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Molecular basis for beta-glucosidase inhibition by ring-modified calystegine analogues.
Aguilar M, Gloster TM, García-Moreno MI, Ortiz Mellet C, Davies GJ, Llebaria A, Casas J, Egido-Gabás M, García Fernandez JM
Chembiochem 9 2612-8 (2008)
PMID: 18833549

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-555165 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucosidase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 468 amino acids
Theoretical weight: 53.94 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q08638 (Residues: 2-446; Coverage: 100%)
Gene name: bglA
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

3 bound ligands:
Ligand NCW 2 x NCW
Ligand CA 2 x CA
Ligand ACT 3 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 93.696Å b: 94.409Å c: 113.026Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.239
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

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