1ms4

X-ray diffraction
2.21Å resolution

Triclinic form of Trypanosoma cruzi trans-sialidase

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.

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-173256 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 648 amino acids
Theoretical weight: 71.39 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q26966 (Residues: 2-635; Coverage: 99%)
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 ID14-1
Spacegroup: P1
Unit cell:
a: 50.95Å b: 74.22Å c: 87.467Å
α: 85.94° β: 84.2° γ: 88.38°
R-values:
R R work R free
0.218 0.215 0.272
Expression system: Escherichia coli