X-ray diffraction
1.45Å resolution

Neuraminidase of A/Brevig Mission/1/1918 H1N1 strain in complex with zanamivir

Source organism: Influenza A virus
Primary publication:
Structural characterization of the 1918 influenza virus H1N1 neuraminidase.
J. Virol. 82 10493-501 (2008)
PMID: 18715929

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Neuraminidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 385 amino acids
Theoretical weight: 42.25 KDa
Source organism: Influenza A virus
Expression system: Trichoplusia ni
  • Canonical: Q9IGQ6 (Residues: 83-467; Coverage: 82%)
Gene name: NA
Sequence domains: Neuraminidase
Structure domains: Neuraminidase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2221
Unit cell:
a: 118.044Å b: 129.247Å c: 118.845Å
α: 90° β: 90° γ: 90°
R R work R free
0.141 0.14 0.16
Expression system: Trichoplusia ni