› 1up4

X-ray diffraction
2.85Å resolution

Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom resolution in the monoclinic form

Released:
DOI: 10.2210/pdb1up4/pdb
PDB entry 1up4 coloured by chain, front view.
PDB entry 1up4 coloured by chain, side view.
PDB entry 1up4 coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
NAD+ and metal-ion dependent hydrolysis by family 4 glycosidases: structural insight into specificity for phospho-beta-D-glucosides.
Varrot A, Yip VL, Li Y, Rajan SS, Yang X, Anderson WF, Thompson J, Withers SG, Davies GJ
J Mol Biol 346 423-35 (2005)
PMID: 15670594

Function and Biology Details

Reaction catalysed: 
6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H(2)O = D-glucose + D-glucose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194761 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-phospho-beta-glucosidase BglT Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 415 amino acids
Theoretical weight: 48.02 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X108 (Residues: 1-415; Coverage: 100%)
Gene names: TM_1281, bglT
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 56 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 99.048Å b: 188.315Å c: 125.628Å
α: 90° β: 104.52° γ: 90°
R-values:
R R work R free
0.198 0.196 0.235
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

3 mentions without citation

Evolution and biochemistry of family 4 glycosidases: implications for assigning enzyme function in sequence annotations.
Hall et al. (2009)
2 more