1ms9

X-ray diffraction
1.58Å resolution

Triclinic form of Trypanosoma cruzi trans-sialidase, in complex with lactose

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-173256 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Trans-sialidase 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:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GAL
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: 51.046Å b: 74.204Å c: 87.496Å
α: 86.02° β: 84.17° γ: 88.31°
R-values:
R R work R free
0.166 0.163 0.198
Expression system: Escherichia coli