8xpd

X-ray diffraction
1.7Å resolution

Crystal structure of Tris-bound TsaBgl (DATA II)

Released:
Model geometry
Fit model/data
Primary publication:
Structural analysis of Tris binding in β-glucosidases.
Biochem Biophys Res Commun 700 149608 (2024)
PMID: 38306932

Function and Biology Details

Reaction catalysed:
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125104 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 444 amino acids
Theoretical weight: 51.79 KDa
Source organism: Thermoanaerobacterium saccharolyticum JW/SL-YS485
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: I3VXG7 (Residues: 1-444; Coverage: 100%)
Gene name: Tsac_2208
Sequence domains: Glycosyl hydrolase family 1

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PAL/PLS BEAMLINE 11C
Spacegroup: P212121
Unit cell:
a: 65.044Å b: 70.95Å c: 99.032Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.152 0.151 0.179
Expression system: Escherichia coli BL21(DE3)