PDBe 1b9v

X-ray diffraction
2.35Å resolution

NOVEL AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE MAKE SELECTIVE INTERACTIONS WITH CONSERVED RESIDUES AND WATER MOLECULES IN TEH ACTIVE SITE

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:
Biological process:
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: 390 amino acids
Theoretical weight: 43.46 KDa
Source organism: Influenza B virus (B/Lee/1940)
UniProt:
  • Canonical: P03474 (Residues: 77-466; Coverage: 84%)
Gene name: NA
Structure domains: Neuraminidase

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P4212
Unit cell:
a: 124.702Å b: 124.702Å c: 71.573Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.271