3nss

X-ray diffraction
1.9Å resolution

The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active sites

Released:

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:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111249 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Neuraminidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 388 amino acids
Theoretical weight: 42.73 KDa
Source organism: Influenza A virus (A/California/04/2009(H1N1))
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: C3W5S3 (Residues: 82-469; Coverage: 83%)
Gene name: NA
Sequence domains: Neuraminidase
Structure domains: Neuraminidase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, MAN
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2221
Unit cell:
a: 118.537Å b: 137.857Å c: 118.512Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.169 0.196
Expression system: Spodoptera frugiperda