› 7s0i

X-ray diffraction
2.89Å 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-102820 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Neuraminidase Chain: A
Molecule details ›
Chain: A
Length: 393 amino acids
Theoretical weight: 43.26 KDa
Source organism: Influenza A virus (A/Michigan/45/2015(H1N1))
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: A0A0X9QTS2 (Residues: 82-469; Coverage: 83%)
Gene name: NA
Sequence domains: Neuraminidase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
2 bound ligands:
Ligand NAG 1 x NAG
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P4212
Unit cell:
a: 92.132Å b: 92.132Å c: 104.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.294 0.292 0.321
Expression system: Spodoptera frugiperda

Quick links

Citations

4 review citations

Influenza and Universal Vaccine Research in China.
Li et al. (2022)
3 more

2 mentions without citation

A Novel Recombinant Influenza Virus Neuraminidase Vaccine Candidate Stabilized by a Measles Virus Phosphoprotein Tetramerization Domain Provides Robust Protection from Virus Challenge in the Mouse Model.
Strohmeier et al. (2021)
1 more