› 1n1s

X-ray diffraction
1.64Å 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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129183 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 641 amino acids
Theoretical weight: 69.91 KDa
Source organism: Trypanosoma rangeli
Expression system: Escherichia coli
UniProt:
  • Canonical: O44049 (Residues: 23-660; Coverage: 100%)
Sequence domains: BNR repeat-like domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P212121
Unit cell:
a: 76.02Å b: 93.97Å c: 105.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.194
Expression system: Escherichia coli

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Citations

5 review citations

Diversity of microbial sialic acid metabolism.
Vimr et al. (2004)
4 more

4 mentions without citation

Unraveling virus relationships by structure-based phylogenetic classification.
Ng et al. (2020)
3 more