› 1w0o

X-ray diffraction
1.9Å resolution

Vibrio cholerae sialidase

Released:
DOI: 10.2210/pdb1w0o/pdb
PDB entry 1w0o coloured by chain, front view.
PDB entry 1w0o coloured by chain, side view.
PDB entry 1w0o coloured by chain, top view.
Source organism: Vibrio cholerae
Primary publication:
Sialic acid recognition by Vibrio cholerae neuraminidase.
Moustafa I, Connaris H, Taylor M, Zaitsev V, Wilson JC, Kiefel MJ, von Itzstein M, Taylor G
J Biol Chem 279 40819-26 (2004)
PMID: 15226294

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143046 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase Chain: A
Molecule details ›
Chain: A
Length: 781 amino acids
Theoretical weight: 85.67 KDa
Source organism: Vibrio cholerae
UniProt:
  • Canonical: P0C6E9 (Residues: 1-781; Coverage: 100%)
Gene names: VC_1784, nanH
Sequence domains: Vibrio cholerae sialidase, lectin insertion
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand DAN 1 x DAN
Ligand CA 4 x CA
Ligand SIA 1 x SIA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 70.31Å b: 74.91Å c: 151.615Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.218

Quick links

Citations

14 review citations

The type II secretion system: biogenesis, molecular architecture and mechanism.
Korotkov et al. (2012)
13 more

9 mentions without citation

Identifying selective inhibitors against the human cytosolic sialidase NEU2 by substrate specificity studies.
Li et al. (2011)
8 more