PDBe 1n1v

X-ray diffraction
2.1Å resolution

Trypanosoma rangeli sialidase in complex with 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.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

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

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 75.862Å b: 93.404Å c: 105.821Å
α: 90° β: 90° γ: 90°
R R work R free
0.18 0.178 0.219
Expression system: Escherichia coli