X-ray diffraction
2.9Å resolution

Trypanosoma rangeli sialidase in complex with the inhibitor DANA


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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Sialidase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 638 amino acids
Theoretical weight: 69.71 KDa
Source organism: Trypanosoma rangeli
  • Canonical: O44049 (Residues: 23-660; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE D41A
Spacegroup: P212121
Unit cell:
a: 76.2Å b: 93.8Å c: 105.3Å
α: 90° β: 90° γ: 90°
R R work R free
0.209 0.205 0.287