› 2hty

X-ray diffraction
2.5Å resolution

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:
PDBe Complex ID:
PDB-CPX-179539 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuraminidase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 387 amino acids
Theoretical weight: 42.43 KDa
Source organism: Influenza A virus
UniProt:
  • Canonical: Q6DPL2 (Residues: 63-449; Coverage: 86%)
Gene name: NA
Sequence domains: Neuraminidase
Structure domains: Neuraminidase

Ligands and Environments

3 bound ligands:
Ligand NDG 7 x NDG
Ligand CA 8 x CA
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 200.21Å b: 200.77Å c: 211.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.232 0.262

Quick links

Citations

74 review citations

Approved Antiviral Drugs over the Past 50 Years.
De Clercq et al. (2016)
73 more

69 mentions without citation

Influenza Hemagglutinin and Neuraminidase: Yin⁻Yang Proteins Coevolving to Thwart Immunity.
Kosik et al. (2019)
68 more