› 2htv

X-ray diffraction
2.8Å 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-180539 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuraminidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 390 amino acids
Theoretical weight: 42.93 KDa
Source organism: Influenza A virus
UniProt:
  • Canonical: Q6XV46 (Residues: 81-470; Coverage: 83%)
Gene name: NA
Sequence domains: Neuraminidase
Structure domains: Neuraminidase

Ligands and Environments

2 bound ligands:
Ligand NAG 2 x NAG
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P432
Unit cell:
a: 193.79Å b: 193.79Å c: 193.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.222 0.273

Quick links

Citations

74 review citations

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

10 mentions without citation

Unraveling virus relationships by structure-based phylogenetic classification.
Ng et al. (2020)
9 more