› 3zjk

X-ray diffraction
2.2Å resolution

crystal structure of Ttb-gly F401S mutant

Released:
DOI: 10.2210/pdb3zjk/pdb
PDB entry 3zjk coloured by chain, front view.
PDB entry 3zjk coloured by chain, side view.
PDB entry 3zjk coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Semi-rational approach for converting a GH1 β-glycosidase into a β-transglycosidase.
Teze D, Hendrickx J, Czjzek M, Ropartz D, Sanejouand YH, Tran V, Tellier C, Dion M
Protein Eng Des Sel 27 13-9 (2014)
PMID: 24287187

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-193124 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucosidase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 431 amino acids
Theoretical weight: 48.61 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: Q9RA61 (Residues: 1-431; Coverage: 100%)
Gene names: b-gly, bglT
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
Ligand GOL 3 x GOL
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 98.557Å b: 77.322Å c: 101.767Å
α: 90° β: 103.46° γ: 90°
R-values:
R R work R free
0.175 0.173 0.223
Expression system: Escherichia coli DH5[alpha]

Quick links

Citations

6 review citations

Synthesis of Human Milk Oligosaccharides: Protein Engineering Strategies for Improved Enzymatic Transglycosylation.
Zeuner et al. (2019)
5 more

1 mention without citation

Engineering a thermostable Halothermothrix orenii β-glucosidase for improved galacto-oligosaccharide synthesis.
Hassan et al. (2016)