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-124812 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Neuraminidase
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 378 amino acids
Theoretical weight: 41.94 KDa
Source organism: Influenza A virus (A/little yellow-shouldered bat/Guatemala/164/2009(H17N10))
Expression system: Spodoptera frugiperda
UniProt:
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
Length: 378 amino acids
Theoretical weight: 41.94 KDa
Source organism: Influenza A virus (A/little yellow-shouldered bat/Guatemala/164/2009(H17N10))
Expression system: Spodoptera frugiperda
UniProt:
- Canonical:
H6QM85 (Residues: 74-442; Coverage: 84%)
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
Ligands and Environments
Experiments and Validation Details
X-ray source:
APS BEAMLINE 22-ID
Spacegroup:
P1
Expression system: Spodoptera frugiperda
