The X-ray structure of a complex of 5-N-acetyl-5-amino-3-(1- ethylpropoxy)-1-cyclohexene-1-carboxylic acid (GS4071) and a drug resistant variant R292K of tern N9 influenza virus neuraminidase

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 43% strand (DSSP).

Ligands and binding sites

• G39 · (3R,4R,5S)-4-(acetylamino)-5-amino-3-(pentan-3-yloxy) cyclohex-1-ene-1-carboxylic acid · ligand · chains A
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
• MAN · alpha-D-mannopyranose · sugar · 4 copies
• BMA · beta-D-mannopyranose · sugar
• CA · Calcium ion · metal · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 9 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

• 2QWH · The X-ray structure of a complex of 5-N-acetyl-5-amino-3-(1-ethylpropoxy)-1-cyclohexene-1… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P03472
• Elsewhere: RCSB PDB 2QWH · PDBe 2QWH · UniProt P03472