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 analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Neuraminidase (preferred)
PDBe Complex ID:
PDB-CPX-174776 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuraminidase
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 397 amino acids
Theoretical weight: 43.84 KDa
Source organism: Influenza B virus (B/Perth/211/2001)
Expression system: Spodoptera frugiperda
UniProt:
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
Length: 397 amino acids
Theoretical weight: 43.84 KDa
Source organism: Influenza B virus (B/Perth/211/2001)
Expression system: Spodoptera frugiperda
UniProt:
- Canonical:
Q3S340 (Residues: 70-466; Coverage: 85%)
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
