PDBe 1kit

X-ray diffraction
2.3Å resolution



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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Sialidase Chain: A
Molecule details ›
Chain: A
Length: 757 amino acids
Theoretical weight: 83.04 KDa
Source organism: Vibrio cholerae
Expression system: Escherichia coli
  • Canonical: P0C6E9 (Residues: 25-781; Coverage: 100%)
Gene names: VC_1784, nanH
Sequence domains: Vibrio cholerae sialidase, lectin insertion
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 72.3Å b: 78.9Å c: 164.5Å
α: 90° β: 90° γ: 90°
R R work R free
0.17 0.17 not available
Expression system: Escherichia coli