› 1b9t

X-ray diffraction
2.4Å resolution

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

Released:
DOI: 10.2210/pdb1b9t/pdb
PDB entry 1b9t coloured by chain, front view.
PDB entry 1b9t coloured by chain, side view.
PDB entry 1b9t coloured by chain, top view.
Source organism: Influenza B virus (B/Lee/1940)
Primary publication:
Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site.
Finley JB, Atigadda VR, Duarte F, Zhao JJ, Brouillette WJ, Air GM, Luo M
J Mol Biol 293 1107-19 (1999)
PMID: 10547289

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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137060 (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
Sequence domains: Neuraminidase
Structure domains: Neuraminidase

Ligands and Environments

3 bound ligands:
Ligand NAG 1 x NAG
Ligand CA 2 x CA
Ligand RAI 1 x RAI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P4212
Unit cell:
a: 124.5Å b: 124.5Å c: 71.412Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.271

Quick links

Citations

2 review citations

Structural glycobiology: a game of snakes and ladders.
DeMarco et al. (2008)
1 more

4 mentions without citation

Bioinformatics studies on a function of the SARS-CoV-2 spike glycoprotein as the binding of host sialic acid glycans.
Robson B. (2020)
3 more