› 2ht5

X-ray diffraction
2.4Å 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-170484 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuraminidase Chain: A
Molecule details ›
Chain: A
Length: 390 amino acids
Theoretical weight: 43.16 KDa
Source organism: Influenza A virus
UniProt:
  • Canonical: Q07599 (Residues: 81-470; Coverage: 83%)
Gene name: NA
Sequence domains: Neuraminidase
Structure domains: Neuraminidase

Ligands and Environments

2 bound ligands:
Ligand NDG 1 x NDG
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I4
Unit cell:
a: 90.52Å b: 90.52Å c: 108.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.261

Quick links

Citations

75 review citations

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

13 mentions without citation

Emerging HxNy Influenza A Viruses.
Liu et al. (2022)
12 more