› 2wc4

X-ray diffraction
1.7Å resolution

Structure of family 1 beta-glucosidase from Thermotoga maritima in complex with 3-imino-2-thia-(+)-castanospermine

Released:
DOI: 10.2210/pdb2wc4/pdb
PDB entry 2wc4 coloured by chain, front view.
PDB entry 2wc4 coloured by chain, side view.
PDB entry 2wc4 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring.
Aguilar-Moncayo M, Gloster TM, Turkenburg JP, García-Moreno MI, Ortiz Mellet C, Davies GJ, García Fernández JM
Org Biomol Chem 7 2738-47 (2009)
PMID: 19532990

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170668 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucosidase A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 468 amino acids
Theoretical weight: 53.94 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08638 (Residues: 2-446; Coverage: 100%)
Gene name: bglA
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

4 bound ligands:
Ligand AMF 4 x AMF
Ligand EDO 6 x EDO
Ligand ACT 1 x ACT
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 89.872Å b: 73.287Å c: 137.979Å
α: 90° β: 94.17° γ: 90°
R-values:
R R work R free
0.169 0.167 0.213
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

1 mention without citation

Aglycone specificity of Thermotoga neapolitana β-glucosidase 1A modified by mutagenesis, leading to increased catalytic efficiency in quercetin-3-glucoside hydrolysis.
Khan et al. (2011)