› 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

73 review citations

Avian influenza virus (H5N1): a threat to human health.
Peiris et al. (2007)
72 more

65 mentions without citation

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