PDBe 2w68

X-ray diffraction
2.5Å resolution

ENHANCING THE RECEPTOR AFFINITY OF THE SIALIC ACID-BINDING DOMAIN OF VIBRIO CHOLERAE SIALIDASE THROUGH MULTIVALENCY

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. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 195 amino acids
Theoretical weight: 21.1 KDa
Source organism: Vibrio cholerae
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C6E9 (Residues: 25-216; Coverage: 25%)
Gene names: VC_1784, nanH
Structure domains: Jelly Rolls

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2221
Unit cell:
a: 138.6Å b: 197.62Å c: 82.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.215 0.256
Expression system: Escherichia coli