PDBe 1n1t

X-ray diffraction
1.6Å resolution

Trypanosoma rangeli sialidase in complex with DANA at 1.6 A

Released:

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
Macromolecule:
Sialidase 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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 73.945Å b: 96.258Å c: 106.513Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.197
Expression system: Escherichia coli