4b7j

X-ray diffraction
2.42Å resolution

H1N1 2009 Pandemic Influenza Virus: Resistance of the I223R Neuraminidase Mutant Explained by Kinetic and Structural Analysis

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuraminidase Chain: A
Molecule details ›
Chain: A
Length: 469 amino acids
Theoretical weight: 51.7 KDa
Source organism: Influenza A virus
Expression system: Gallus gallus
UniProt:
  • Canonical: F8UU09 (Residues: 1-469; Coverage: 100%)
Gene name: NA
Sequence domains: Neuraminidase
Structure domains: Neuraminidase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P4212
Unit cell:
a: 118.55Å b: 118.55Å c: 67.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.233
Expression system: Gallus gallus