Fluorine in PDB 7as2: Influenza A PB2 (M431 Mutation) in Complex with Vx-787

The structure of Influenza A PB2 (M431 Mutation) in Complex with Vx-787, PDB code: 7as2 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)	24.34 / 1.75
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	29.19, 37.12, 38.45, 71.85, 75.39, 75.92
R / Rfree (%)	16 / 20.5

The binding sites of Fluorine atom in the Influenza A PB2 (M431 Mutation) in Complex with Vx-787 (pdb code 7as2). 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 (M431 Mutation) in Complex with Vx-787, PDB code: 7as2:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Influenza A PB2 (M431 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 (M431 Mutation) in Complex with Vx-787 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:23.0 occ:1.00 F31 A:21G501 0.0 23.0 1.0 C14 A:21G501 1.4 18.9 1.0 C15 A:21G501 2.4 16.4 1.0 C13 A:21G501 2.4 19.5 1.0 N17 A:21G501 2.8 16.8 1.0 O A:HOH719 3.0 29.9 1.0 N16 A:21G501 3.6 15.3 1.0 CD2 A:PHE323 3.6 19.1 1.0 N12 A:21G501 3.7 15.8 1.0 O A:HOH741 3.7 24.9 0.5 CG A:PHE323 3.9 19.0 1.0 C11 A:21G501 4.1 15.0 1.0 CE2 A:PHE323 4.1 18.3 1.0 CB A:PHE323 4.2 19.0 1.0 C18 A:21G501 4.3 17.1 1.0 CD1 A:PHE323 4.6 18.6 1.0 CZ A:PHE323 4.8 17.8 1.0 C20 A:21G501 5.0 19.6 1.0

Fluorine binding site 2 out of 2 in the Influenza A PB2 (M431 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 (M431 Mutation) in Complex with Vx-787 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:13.5 occ:1.00 F32 A:21G501 0.0 13.5 1.0 C2 A:21G501 1.4 13.8 1.0 C3 A:21G501 2.4 14.4 1.0 C1 A:21G501 2.4 13.8 1.0 NE2 A:GLN406 3.3 11.2 1.0 O A:PHE404 3.3 9.8 1.0 N4 A:21G501 3.6 13.5 1.0 CD A:GLN406 3.6 11.9 1.0 C6 A:21G501 3.6 13.3 1.0 CG A:GLN406 3.7 11.3 1.0 O A:HOH670 3.8 19.0 0.5 CD1 A:PHE404 3.9 11.3 1.0 C26 A:21G501 3.9 16.4 1.0 C5 A:21G501 4.1 13.2 1.0 CE1 A:PHE404 4.1 12.5 1.0 C A:PHE404 4.2 10.3 1.0 CA A:PHE404 4.2 10.7 1.0 OE1 A:GLN406 4.3 12.2 1.0 CG A:PHE404 4.3 11.4 1.0 CG2 A:ILE431 4.4 15.5 1.0 CG1 A:ILE431 4.5 15.0 1.0 CD2 A:HIS357 4.6 15.2 1.0 CZ A:PHE404 4.6 12.4 1.0 CD1 A:ILE431 4.7 16.4 1.0 C25 A:21G501 4.7 17.0 1.0 C27 A:21G501 4.8 17.2 1.0 CB A:PHE404 4.9 10.7 1.0 CD2 A:PHE404 4.9 11.4 1.0 C7 A:21G501 4.9 13.8 1.0 CE2 A:PHE404 5.0 12.3 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