Chlorine in PDB 7ltj: Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease (3CL Mpro) in Complex with A Non-Covalent Inhibitor Mcule-5948770040

All present enzymatic activity of Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease (3CL Mpro) in Complex with A Non-Covalent Inhibitor Mcule-5948770040:
3.4.22.69;

The structure of Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease (3CL Mpro) in Complex with A Non-Covalent Inhibitor Mcule-5948770040, PDB code: 7ltj was solved by A.Kovalevsky, D.W.Kneller, L.Coates, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.93 / 1.80
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	55.231, 81.466, 88.808, 90, 96.56, 90
R / Rfree (%)	16.2 / 19.2

The binding sites of Chlorine atom in the Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease (3CL Mpro) in Complex with A Non-Covalent Inhibitor Mcule-5948770040 (pdb code 7ltj). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease (3CL Mpro) in Complex with A Non-Covalent Inhibitor Mcule-5948770040, PDB code: 7ltj:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease (3CL Mpro) in Complex with A Non-Covalent Inhibitor Mcule-5948770040


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease (3CL Mpro) in Complex with A Non-Covalent Inhibitor Mcule-5948770040 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:43.0 occ:1.00 CL15 A:YD1401 0.0 43.0 1.0 C14 A:YD1401 1.8 40.9 1.0 C16 A:YD1401 2.7 32.2 1.0 C13 A:YD1401 2.7 40.6 1.0 CL17 A:YD1401 3.2 44.2 1.0 N A:ARG188 3.7 31.7 1.0 C A:ASP187 3.7 38.5 1.0 CA A:ASP187 3.8 24.4 1.0 C A:ARG188 3.8 46.1 1.0 SD A:MET165 3.8 41.5 1.0 O A:ARG188 3.8 39.8 1.0 C12 A:YD1401 4.0 36.0 1.0 C10 A:YD1401 4.0 34.2 1.0 CA A:ARG188 4.1 40.3 1.0 CD2 A:HIS41 4.2 25.5 1.0 N A:GLN189 4.2 50.4 1.0 CB A:ASP187 4.2 28.1 1.0 O A:ASP187 4.3 34.2 1.0 CG A:GLN189 4.3 59.3 1.0 CB A:MET165 4.3 28.0 1.0 C11 A:YD1401 4.5 39.7 1.0 CA A:GLN189 4.6 49.4 1.0 OE1 A:GLN189 4.7 73.0 1.0 O A:VAL186 4.7 27.3 1.0 CG A:MET165 4.7 28.3 1.0 CD A:GLN189 4.8 73.5 1.0 O A:HIS164 4.8 27.8 1.0 CG A:HIS41 4.8 29.3 1.0 NE2 A:HIS41 4.9 31.0 1.0

Chlorine binding site 2 out of 2 in the Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease (3CL Mpro) in Complex with A Non-Covalent Inhibitor Mcule-5948770040


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease (3CL Mpro) in Complex with A Non-Covalent Inhibitor Mcule-5948770040 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:44.2 occ:1.00 CL17 A:YD1401 0.0 44.2 1.0 C13 A:YD1401 1.7 40.6 1.0 C12 A:YD1401 2.7 36.0 1.0 C14 A:YD1401 2.8 40.9 1.0 CL15 A:YD1401 3.2 43.0 1.0 O A:ASP187 3.4 34.2 1.0 OH A:TYR54 3.4 34.9 1.0 CB A:HIS41 3.6 24.7 1.0 C A:ASP187 3.8 38.5 1.0 CA A:ARG188 3.8 40.3 1.0 C11 A:YD1401 4.0 39.7 1.0 C16 A:YD1401 4.0 32.2 1.0 N A:ARG188 4.1 31.7 1.0 N A:GLN189 4.1 50.4 1.0 C A:ARG188 4.3 46.1 1.0 CG A:GLN189 4.3 59.3 1.0 CG A:HIS41 4.3 29.3 1.0 O A:MET49 4.3 53.3 1.0 SG A:CYS44 4.3 45.1 1.0 CG A:MET49 4.4 61.1 1.0 CA A:MET49 4.5 57.3 1.0 CD2 A:HIS41 4.5 25.5 1.0 CB A:MET49 4.5 54.9 1.0 C10 A:YD1401 4.6 34.2 1.0 CG A:PRO52 4.7 47.6 1.0 CA A:ASP187 4.8 24.4 1.0 CZ A:TYR54 4.8 31.3 1.0 CB A:ASP187 4.8 28.1 1.0 CA A:HIS41 4.9 28.9 1.0 C A:MET49 4.9 61.9 1.0 CB A:CYS44 4.9 41.1 1.0

A.Clyde, S.Galanie, D.W.Kneller, H.Ma, V.Kertesz, L.Coates, A.Brace, A.Trifan, B.Blaiszik, K.Chard, R.Chard, Z.Li, Y.Babuji, I.Foster, T.Brettin, H.Lee, A.Merzky, M.Titov, M.Turilli, L.Tan, H.Van Dam, J.Schmidt, S.Jha, A.Kovalevsky, A.Ramanathan, M.Head, R.Stevens. High Throughput Virtual Screening and Validation of A Non-Covalent Inhibitor of the Sars-Cov-2 Main Protease To Be Published.