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-170484 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuraminidase
Molecule details ›
Chain: A
Length: 390 amino acids
Theoretical weight: 43.2 KDa
Source organism: Influenza A virus (A/duck/Ukraine/1/1963(H3N8))
Expression system: Escherichia coli
UniProt:
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
Length: 390 amino acids
Theoretical weight: 43.2 KDa
Source organism: Influenza A virus (A/duck/Ukraine/1/1963(H3N8))
Expression system: Escherichia coli
UniProt:
- Canonical:
Q07599 (Residues: 81-470; Coverage: 83%)
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
