Fluorine in PDB 7awr: Structure of Sars-Cov-2 Main Protease Bound to Tegafur

All present enzymatic activity of Structure of Sars-Cov-2 Main Protease Bound to Tegafur:
2.7.7.48; 3.4.19.12; 3.4.22.69; 3.6.4.12; 3.6.4.13;

The structure of Structure of Sars-Cov-2 Main Protease Bound to Tegafur, PDB code: 7awr was solved by S.Guenther, P.Y.A.Reinke, D.Oberthuer, O.Yefanov, L.Gelisio, H.Ginn, J.Lieske, M.Domaracky, W.Brehm, A.Rahmani Mashour, T.A.White, J.Knoska, G.Pena Esperanza, F.Koua, A.Tolstikova, M.Groessler, P.Fischer, V.Hennicke, H.Fleckenstein, F.Trost, M.Galchenkova, Y.Gevorkov, C.Li, S.Awel, L.X.Paulraj, N.Ullah, S.Falke, B.Alves Franca, M.Schwinzer, H.Brognaro, N.Werner, M.Perbandt, H.Tidow, B.Seychell, T.Beck, S.Meier, J.J.Doyle, H.Giseler, D.Melo, T.J.Lane, I.Dunkel, A.Peck, S.Saouane, J.Hakanpaeae, J.Meyer, H.Noei, P.Gribbon, B.Ellinger, M.Kuzikov, M.Wolf, L.Zhang, C.Ehrt, J.Pletzer-Zelgert, J.Wollenhaupt, C.Feiler, M.Weiss, E.C.Schulz, P.Mehrabi, B.Norton-Baker, C.Schmidt, K.Lorenzen, R.Schubert, H.Han, A.Chari, Y.Fernandez Garcia, D.Turk, R.Hilgenfeld, M.Rarey, A.Zaliani, H.N.Chapman, A.Pearson, C.Betzel, A.Meents, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.49 / 1.34
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	112.915, 52.973, 44.763, 90.00, 102.94, 90.00
R / Rfree (%)	15.2 / 19.2

The binding sites of Fluorine atom in the Structure of Sars-Cov-2 Main Protease Bound to Tegafur (pdb code 7awr). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Structure of Sars-Cov-2 Main Protease Bound to Tegafur, PDB code: 7awr:

Fluorine binding site 1 out of 1 in the Structure of Sars-Cov-2 Main Protease Bound to Tegafur


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Sars-Cov-2 Main Protease Bound to Tegafur within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:69.2 occ:0.50 F14 A:S7W401 0.0 69.2 0.5 C08 A:S7W401 1.3 81.0 0.5 H22 A:DMS402 1.6 57.6 0.5 H21 A:DMS402 1.7 57.6 0.5 C2 A:DMS402 1.9 48.0 0.5 C07 A:S7W401 2.3 26.1 0.5 C09 A:S7W401 2.4 57.6 0.5 H23 A:DMS402 2.4 57.6 0.5 HA A:LYS102 2.6 30.3 0.5 HA A:LYS102 2.6 28.8 0.5 H071 A:S7W401 2.6 31.2 0.5 O10 A:S7W401 2.8 0.4 0.5 O A:HOH661 2.9 33.7 1.0 O A:TYR101 3.2 25.7 1.0 HE2 A:TYR101 3.3 31.8 1.0 CE2 A:TYR101 3.5 26.5 1.0 CA A:LYS102 3.5 25.3 0.5 CA A:LYS102 3.5 24.0 0.5 S A:DMS402 3.6 58.1 0.5 H A:PHE103 3.6 27.2 1.0 N11 A:S7W401 3.6 40.1 0.5 HD2 A:TYR101 3.6 30.1 1.0 N06 A:S7W401 3.6 49.4 0.5 CD2 A:TYR101 3.7 25.1 1.0 C A:TYR101 3.9 25.6 1.0 N A:PHE103 4.1 22.6 1.0 N A:LYS102 4.1 26.6 0.5 N A:LYS102 4.1 25.8 0.5 C12 A:S7W401 4.1 92.8 0.5 C A:LYS102 4.2 23.0 0.5 C A:LYS102 4.2 24.4 0.5 CZ A:TYR101 4.2 26.2 1.0 HG2 A:LYS102 4.2 41.0 0.5 HG2 A:LYS102 4.2 37.0 0.5 H13 A:DMS402 4.4 28.7 0.5 H111 A:S7W401 4.4 48.1 0.5 C1 A:DMS402 4.5 23.9 0.5 H12 A:DMS402 4.5 28.7 0.5 O A:DMS402 4.5 60.1 0.5 CB A:LYS102 4.5 28.0 0.5 CB A:LYS102 4.5 26.3 0.5 CG A:TYR101 4.6 23.2 1.0 HB3 A:LYS102 4.7 33.6 0.5 HB3 A:LYS102 4.7 31.5 0.5 OH A:TYR101 4.7 29.3 1.0 CG A:LYS102 4.7 34.2 0.5 O04 A:S7W401 4.7 36.9 0.5 CG A:LYS102 4.8 30.9 0.5 HG3 A:LYS102 4.8 41.0 0.5 HG3 A:LYS102 4.9 37.0 0.5 H A:LYS102 4.9 32.0 0.5 C03 A:S7W401 4.9 55.5 0.5 H A:LYS102 4.9 31.0 0.5 HB2 A:PHE103 4.9 25.2 1.0 O A:HOH647 4.9 40.8 1.0 CE1 A:TYR101 5.0 26.4 1.0

S.Guenther, P.Y.A., Reinke, Y., Fernandez-Garcia, J., Lieske, T.J., Lane, H.M., Ginn, F.H.M., Koua, C., Ehrt, W., Ewert, D., Oberthuer, O., Yefanov, S., Meier, K., Lorenzen, B., Krichel, J.D., Kopicki, L., Gelisio, W., Brehm, I., Dunkel, B., Seychell, H., Gieseler, B., Norton-Baker, B., Escudero-Perez, M., Domaracky, S., Saouane, A., Tolstikova, T.A., White, A., Hanle, M., Groessler, H., Fleckenstein, F., Trost, M., Galchenkova, Y., Gevorkov, C., Li, S., Awel, A.Peck, M., Barthelmess, F., Schluenzen, L.X., Paulraj, N., Werner, H., Andaleeb, N., Ullah, S., Falke, V., Srinivasan, B., Franca, M., Schwinzer, H., Brognaro, C., Rogers, D., Melo, J.J., Doyle, J., Knoska, G.E., Pena Murillo, A., Rahmani Mashhour, F., Guicking, V., Hennicke, P., Fischer, J., Hakanpaeae, J., Meyer, P., Gribbon, B., Ellinger, M., Kuzikov, M., Wolf, G., Burenkov, D., Von Stetten, G., Pompidor, I., Bento, S., Panneerselvam, I., Karpics, T.R., Schneider, M., Garcia Alai, S., Niebling, C., Guenther, C., Schmidt, R., Schubert, H., Han, J., Boger, D., Monteiro, L., Zhang, X., Sun, J., Pletzer-Zelgert, J., Wollenhaupt, C., Feiler, M., Weiss, E.C., Schulz, P., Mehrabi, K., Karnicar, A., Usenik, J., Loboda, H., Tidow, A., Chari, R., Hilgenfeld, C., Uetrecht, R., Cox, A., Zaliani, T., Beck, M., Rarey, S., Guenther, D., Turk, W., Hinrichs, H.N., Chapman, A., Pearson, C., Betzel, A.Meents. Inhibition of Sars-Cov-2 Main Protease By Allosteric Drug-Binding Biorxiv 2020.
DOI: 10.1101/2020.11.12.378422