Fluorine in PDB 7as1: Influenza A PB2 (F404Y Mutation) in Complex with Vx-787

The structure of Influenza A PB2 (F404Y Mutation) in Complex with Vx-787, PDB code: 7as1 was solved by K.Radilova, J.Brynda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.93 / 1.50
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	29.5, 37.25, 38.39, 71.89, 69.8, 75.17
R / Rfree (%)	15 / 18.5

The structure of Influenza A PB2 (F404Y Mutation) in Complex with Vx-787 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the Influenza A PB2 (F404Y Mutation) in Complex with Vx-787 (pdb code 7as1). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Influenza A PB2 (F404Y Mutation) in Complex with Vx-787, PDB code: 7as1:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Influenza A PB2 (F404Y Mutation) in Complex with Vx-787


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Influenza A PB2 (F404Y Mutation) in Complex with Vx-787 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:19.4 occ:0.94 F31 A:21G501 0.0 19.4 0.9 C14 A:21G501 1.4 16.5 1.0 C13 A:21G501 2.3 15.2 1.0 C15 A:21G501 2.4 14.6 1.0 N17 A:21G501 2.8 15.7 1.0 O A:HOH743 3.0 18.5 1.0 N12 A:21G501 3.6 14.4 1.0 N16 A:21G501 3.6 13.0 1.0 O A:HOH685 3.6 27.3 0.5 CG A:PHE323 3.7 16.8 1.0 CD1 A:PHE323 3.7 20.6 1.0 C11 A:21G501 4.0 13.7 1.0 CB A:PHE323 4.1 14.9 1.0 CD2 A:PHE323 4.1 17.2 1.0 CE1 A:PHE323 4.2 21.1 1.0 C18 A:21G501 4.3 15.8 1.0 CE2 A:PHE323 4.5 17.5 1.0 CZ A:PHE323 4.6 19.9 1.0

Fluorine binding site 2 out of 2 in the Influenza A PB2 (F404Y Mutation) in Complex with Vx-787


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Influenza A PB2 (F404Y Mutation) in Complex with Vx-787 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:15.3 occ:0.99 F32 A:21G501 0.0 15.3 1.0 C2 A:21G501 1.3 14.2 1.0 C1 A:21G501 2.3 14.6 1.0 C3 A:21G501 2.4 12.9 1.0 O A:TYR404 3.3 11.0 1.0 CE A:MET431 3.3 15.0 1.0 NE2 A:GLN406 3.4 12.0 1.0 CD A:GLN406 3.6 11.8 1.0 C6 A:21G501 3.6 12.3 1.0 N4 A:21G501 3.6 12.6 1.0 CG A:GLN406 3.8 10.9 1.0 C26 A:21G501 3.8 18.0 1.0 CD1 A:TYR404 3.9 12.2 1.0 O A:HOH733 4.0 25.9 1.0 C5 A:21G501 4.0 11.5 1.0 CE1 A:TYR404 4.1 11.5 1.0 C A:TYR404 4.2 9.8 1.0 OE1 A:GLN406 4.2 12.7 1.0 CA A:TYR404 4.2 9.9 1.0 CG A:TYR404 4.2 10.7 1.0 SD A:MET431 4.3 13.3 1.0 CZ A:TYR404 4.6 12.5 1.0 CD2 A:HIS357 4.6 17.2 1.0 CG A:MET431 4.7 12.9 1.0 CD2 A:TYR404 4.7 10.7 1.0 C25 A:21G501 4.7 17.4 1.0 C27 A:21G501 4.8 17.6 1.0 CB A:TYR404 4.8 10.1 1.0 CE2 A:TYR404 4.8 11.6 1.0 C7 A:21G501 5.0 12.6 1.0

J.Gregor, K.Radilova, J.Brynda, J.Fanfrlik, J.Konvalinka, M.Kozisek. Structural and Thermodynamic Analysis of the Resistance Development to Pimodivir (Vx-787), the Clinical Inhibitor of Cap Binding to PB2 Subunit of Influenza A Polymerase Molecules 2021.
ISSN: ESSN 1420-3049
DOI: 10.3390/MOLECULES26041007