Chlorine in PDB 8h3g: Crystal Structure of Sars-Cov-2 Main Protease (Mpro) E166V Mutant in Complex with Inhibitor Enstrelvir

All present enzymatic activity of Crystal Structure of Sars-Cov-2 Main Protease (Mpro) E166V Mutant in Complex with Inhibitor Enstrelvir:
3.4.22.69;

The structure of Crystal Structure of Sars-Cov-2 Main Protease (Mpro) E166V Mutant in Complex with Inhibitor Enstrelvir, PDB code: 8h3g was solved by H.Wang, M.Lin, Y.Duan, X.Zhang, H.Zhou, Q.Bian, X.Liu, Z.Rao, H.Yang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.93 / 1.46
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	55.785, 99.291, 58.933, 90, 108.28, 90
R / Rfree (%)	14.1 / 16.2

The structure of Crystal Structure of Sars-Cov-2 Main Protease (Mpro) E166V Mutant in Complex with Inhibitor Enstrelvir also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Chlorine atom in the Crystal Structure of Sars-Cov-2 Main Protease (Mpro) E166V Mutant in Complex with Inhibitor Enstrelvir (pdb code 8h3g). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Sars-Cov-2 Main Protease (Mpro) E166V Mutant in Complex with Inhibitor Enstrelvir, PDB code: 8h3g:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Sars-Cov-2 Main Protease (Mpro) E166V Mutant in Complex with Inhibitor Enstrelvir


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Sars-Cov-2 Main Protease (Mpro) E166V Mutant in Complex with Inhibitor Enstrelvir within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:21.9 occ:1.00 CL2 A:7YY401 0.0 21.9 1.0 C22 A:7YY401 1.8 18.8 1.0 C21 A:7YY401 2.7 19.6 1.0 C13 A:7YY401 2.8 19.1 1.0 N12 A:7YY401 3.1 21.9 1.0 N10 A:7YY401 3.2 21.3 1.0 C11 A:7YY401 3.3 19.5 1.0 SG A:CYS145 3.4 18.7 1.0 CB A:CYS145 3.5 15.5 1.0 CD2 A:HIS41 3.8 22.4 1.0 C34 A:7YY401 3.9 20.1 1.0 CD2 A:LEU27 4.0 20.7 1.0 C20 A:7YY401 4.0 20.7 1.0 C08 A:7YY401 4.0 21.1 1.0 C14 A:7YY401 4.1 22.7 1.0 N24 A:7YY401 4.2 19.1 1.0 F33 A:7YY401 4.4 20.9 1.0 C32 A:7YY401 4.5 19.6 1.0 C15 A:7YY401 4.5 20.6 1.0 CB A:LEU27 4.6 17.9 1.0 CG A:HIS41 4.6 22.3 1.0 O09 A:7YY401 4.6 21.5 1.0 CB A:HIS41 4.7 21.6 1.0 O A:HOH687 4.7 27.4 1.0 O A:THR26 4.8 20.9 1.0 C26 A:7YY401 4.8 20.0 1.0 N07 A:7YY401 4.8 20.4 1.0 CG A:LEU27 4.8 17.9 1.0 NE2 A:HIS41 4.8 24.8 1.0 C35 A:7YY401 4.9 19.7 1.0 O A:HOH608 4.9 26.2 1.0 C25 A:7YY401 4.9 22.9 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Sars-Cov-2 Main Protease (Mpro) E166V Mutant in Complex with Inhibitor Enstrelvir


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Sars-Cov-2 Main Protease (Mpro) E166V Mutant in Complex with Inhibitor Enstrelvir within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl402 b:24.1 occ:1.00 CL2 B:7YY402 0.0 24.1 1.0 C22 B:7YY402 1.8 21.6 1.0 C21 B:7YY402 2.7 22.8 1.0 C13 B:7YY402 2.8 28.1 1.0 N12 B:7YY402 3.1 27.8 1.0 N10 B:7YY402 3.2 24.1 1.0 C11 B:7YY402 3.3 23.4 1.0 SG B:CYS145 3.5 21.1 1.0 CB B:CYS145 3.6 19.2 1.0 CD2 B:HIS41 3.7 26.8 1.0 O B:HOH711 3.9 58.9 1.0 C34 B:7YY402 3.9 23.3 1.0 C20 B:7YY402 4.0 22.7 1.0 C14 B:7YY402 4.1 28.7 1.0 C08 B:7YY402 4.1 22.5 1.0 CD2 B:LEU27 4.1 21.6 1.0 N24 B:7YY402 4.2 22.2 1.0 F33 B:7YY402 4.4 25.5 1.0 C32 B:7YY402 4.5 23.7 1.0 CG B:HIS41 4.6 26.1 1.0 C15 B:7YY402 4.6 29.2 1.0 CB B:LEU27 4.6 19.1 1.0 O09 B:7YY402 4.6 23.1 1.0 CB B:HIS41 4.7 23.9 1.0 NE2 B:HIS41 4.8 28.8 1.0 C26 B:7YY402 4.8 23.2 1.0 O B:HOH652 4.8 32.0 1.0 O B:THR26 4.8 24.0 1.0 O B:HOH597 4.8 28.6 1.0 N07 B:7YY402 4.8 19.8 1.0 CG B:LEU27 4.9 20.4 1.0 C35 B:7YY402 4.9 22.7 1.0 C25 B:7YY402 4.9 25.8 1.0

Y.Duan, H.Zhou, X.Liu, S.Iketani, M.Lin, X.Zhang, Q.Bian, H.Wang, H.Sun, S.J.Hong, B.Culbertson, H.Mohri, M.I.Luck, Y.Zhu, X.Liu, Y.Lu, X.Yang, K.Yang, Y.Sabo, A.Chavez, S.P.Goff, Z.Rao, D.D.Ho, H.Yang. Molecular Mechanisms of Sars-Cov-2 Resistance to Nirmatrelvir. Nature 2023.
ISSN: ESSN 1476-4687
PubMed: 37696289
DOI: 10.1038/S41586-023-06609-0