› 7qxo

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124636 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
exo-alpha-sialidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 519 amino acids
Theoretical weight: 57.35 KDa
Source organism: Tannerella forsythia
Expression system: Escherichia coli
UniProt:
  • Canonical: G8UIQ1 (Residues: 21-539; Coverage: 96%)
Gene name: BFO_2207
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand GHD 2 x GHD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P41212
Unit cell:
a: 79.868Å b: 79.868Å c: 349.449Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.252 0.29
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Gut Microbial Sialidases and Their Role in the Metabolism of Human Milk Sialylated Glycans.
Muñoz-Provencio et al. (2023)
1 other article

1 mention without citation

Structural and functional characterisation of a stable, broad-specificity multimeric sialidase from the oral pathogen Tannerella forsythia.
Satur et al. (2022)