PDBe 1wcs

X-ray diffraction
2.8Å resolution

A mutant of Trypanosoma rangeli sialidase displaying trans-sialidase activity

Released:
Source organism: Trypanosoma rangeli
Primary publication:
A sialidase mutant displaying trans-sialidase activity.
J. Mol. Biol. 345 923-34 (2005)
PMID: 15588836

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
Macromolecule:
Sialidase Chain: A
Molecule details ›
Chain: A
Length: 641 amino acids
Theoretical weight: 70.07 KDa
Source organism: Trypanosoma rangeli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O44049 (Residues: 20-660; Coverage: 100%)
Sequence domains: BNR repeat-like domain
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P43212
Unit cell:
a: 94.691Å b: 94.691Å c: 156.335Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.244 0.336
Expression system: Escherichia coli BL21