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:
homo tetramer (preferred)
Assembly name:
Neuraminidase (preferred)
PDBe Complex ID:
PDB-CPX-172754 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Neuraminidase
Molecule details ›
Chains: A, B
Length: 388 amino acids
Theoretical weight: 43.05 KDa
Source organism: Influenza A virus (A/RI/5+/1957(H2N2))
Expression system: Spodoptera frugiperda
UniProt:
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
Length: 388 amino acids
Theoretical weight: 43.05 KDa
Source organism: Influenza A virus (A/RI/5+/1957(H2N2))
Expression system: Spodoptera frugiperda
UniProt:
- Canonical:
Q194T1 (Residues: 82-469; Coverage: 83%)
Sequence domains: Neuraminidase
Structure domains: Neuraminidase
Ligands and Environments
1 bound ligand:
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup:
C2221
Expression system: Spodoptera frugiperda
