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:
hetero 24-mer (preferred)
PDBe Complex ID:
PDB-CPX-207760 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Neuraminidase
Molecule details ›
Chains: A, B
Length: 386 amino acids
Theoretical weight: 42.48 KDa
Source organism: Influenza A virus
Expression system: Trichoplusia ni
UniProt:
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
Length: 386 amino acids
Theoretical weight: 42.48 KDa
Source organism: Influenza A virus
Expression system: Trichoplusia ni
UniProt:
- Canonical:
D5KL82 (Residues: 82-467; Coverage: 82%)
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
Immunoglobulin kappa constant
Molecule details ›
Chains: F, L
Length: 212 amino acids
Theoretical weight: 23.27 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Length: 212 amino acids
Theoretical weight: 23.27 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
- Canonical: P01837 (Residues: 1-106; Coverage: 99%)
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
