› 1mz6

X-ray diffraction
2.9Å resolution

Trypanosoma rangeli sialidase in complex with the inhibitor DANA

Released:
DOI: 10.2210/pdb1mz6/pdb
PDB entry 1mz6 coloured by chain, front view.
PDB entry 1mz6 coloured by chain, side view.
PDB entry 1mz6 coloured by chain, top view.
Source organism: Trypanosoma rangeli
Primary publication:
Structural basis of sialyltransferase activity in trypanosomal sialidases.
Buschiazzo A, Tavares GA, Campetella O, Spinelli S, Cremona ML, París G, Amaya MF, Frasch AC, Alzari PM
EMBO J 19 16-24 (2000)
PMID: 10619840

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129183 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 638 amino acids
Theoretical weight: 69.71 KDa
Source organism: Trypanosoma rangeli
UniProt:
  • Canonical: O44049 (Residues: 23-660; Coverage: 100%)
Sequence domains: BNR repeat-like domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NAG 5 x NAG
Ligand DAN 1 x DAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE D41A
Spacegroup: P212121
Unit cell:
a: 76.2Å b: 93.8Å c: 105.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.205 0.287

Quick links

Citations

7 review citations

Achievements and challenges of sialic acid research.
Schauer R. (2000)
6 more

1 mention without citation

The structure of Clostridium perfringens NanI sialidase and its catalytic intermediates.
Newstead et al. (2008)