Function and Biology Details
Reaction catalysed:
[Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidiclinkages of terminal sialic acid residues in oligosaccharides,glycoproteins, glycolipids, colominic acid and synthetic substrates., Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidiclinkages of terminal sialic acid residues in oligosaccharides,glycoproteins, glycolipids, colominic acid and synthetic substrates., Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidiclinkages of terminal sialic acid residues in oligosaccharides,glycoproteins, glycolipids, colominic acid and synthetic substrates., Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidiclinkages of terminal sialic acid residues in oligosaccharides,glycoproteins, glycolipids, colominic acid and synthetic substrates.]
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-304900 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (6 distinct):
Neuraminidase
Molecule details ›
Chains: A, B, C, D
Length: 387 amino acids
Theoretical weight: 42.71 KDa
Source organism: Influenza A virus
Expression system: Homo sapiens
UniProt:
Sequence domains: Neuraminidase
Length: 387 amino acids
Theoretical weight: 42.71 KDa
Source organism: Influenza A virus
Expression system: Homo sapiens
UniProt:
- Canonical:
A0A2P1E3B1 (Residues: 83-469; Coverage: 83%)
Sequence domains: Neuraminidase
Ligands and Environments
No modified residues
