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Chlorine in PDB 9cmu: Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease Drug Resistant Mutant (L50F, E166V) in Complex with Ensitrelvir (Esv)Enzymatic activity of Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease Drug Resistant Mutant (L50F, E166V) in Complex with Ensitrelvir (Esv)
All present enzymatic activity of Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease Drug Resistant Mutant (L50F, E166V) in Complex with Ensitrelvir (Esv):
3.4.22.69; Protein crystallography data
The structure of Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease Drug Resistant Mutant (L50F, E166V) in Complex with Ensitrelvir (Esv), PDB code: 9cmu
was solved by
A.Kovalevsky,
L.Coates,
O.Gerlits,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 9cmu:
The structure of Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease Drug Resistant Mutant (L50F, E166V) in Complex with Ensitrelvir (Esv) also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease Drug Resistant Mutant (L50F, E166V) in Complex with Ensitrelvir (Esv)
(pdb code 9cmu). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease Drug Resistant Mutant (L50F, E166V) in Complex with Ensitrelvir (Esv), PDB code: 9cmu: Chlorine binding site 1 out of 1 in 9cmuGo back to Chlorine Binding Sites List in 9cmu
Chlorine binding site 1 out
of 1 in the Room-Temperature X-Ray Structure of Sars-Cov-2 Main Protease Drug Resistant Mutant (L50F, E166V) in Complex with Ensitrelvir (Esv)
Mono view Stereo pair view
Reference:
A.Kovalevsky,
A.Aniana,
R.Ghirlando,
L.Coates,
V.N.Drago,
L.Wear,
O.Gerlits,
N.T.Nashed,
J.M.Louis.
Effects of Sars-Cov-2 Main Protease Mutations at Positions L50, E166, and L167 Rendering Resistance to Covalent and Noncovalent Inhibitors. J.Med.Chem. 2024.
Page generated: Thu Oct 31 18:10:27 2024
ISSN: ISSN 0022-2623 PubMed: 39370853 DOI: 10.1021/ACS.JMEDCHEM.4C01781 |
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