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
Assemblies composition:
PDBe Complex ID:
PDB-CPX-208657 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Neuraminidase
Molecule details ›
Chain: N
Length: 389 amino acids
Theoretical weight: 43.84 KDa
Source organism: Influenza A virus (A/tern/Australia/G70C/1975(H11N9))
UniProt:
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
Length: 389 amino acids
Theoretical weight: 43.84 KDa
Source organism: Influenza A virus (A/tern/Australia/G70C/1975(H11N9))
UniProt:
- Canonical:
P03472 (Residues: 82-470; Coverage: 83%)
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
Ig gamma-2A chain C region, membrane-bound form
Molecule details ›
Chain: H
Length: 221 amino acids
Theoretical weight: 23.63 KDa
Source organism: Mus musculus
UniProt:
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Length: 221 amino acids
Theoretical weight: 23.63 KDa
Source organism: Mus musculus
UniProt:
- Canonical: P01865 (Residues: 1-100; Coverage: 25%)
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Ligands and Environments
No modified residues
Experiments and Validation Details
Spacegroup:
P4212
