Author: Rui Xiong; Leike Zhang; Shiliang Li; Yuan Sun; Minyi Ding; Yong Wang; Yongliang Zhao; Yan Wu; Weijuan Shang; Xiaming Jiang; Jiwei Shan; Zihao Shen; Yi Tong; Liuxin Xu; Chen Yu; Yingle Liu; Gang Zou; Dimitri Lavillete; Zhenjiang Zhao; Rui Wang; Lili Zhu; Gengfu Xiao; Ke Lan; Honglin Li; Ke Xu
Title: Novel and potent inhibitors targeting DHODH, a rate-limiting enzyme in de novo pyrimidine biosynthesis, are broad-spectrum antiviral against RNA viruses including newly emerged coronavirus SARS-CoV-2 Document date: 2020_3_12
ID: hq5um68k_7
Snippet: ( Supplementary Data Fig. 1A, Table S1 ), we verified the binding mode of S416 at the ubiquinone-binding site of DHODH that similar to S312. The binding free energies for S312 and S416 were -45.06 and -46.74 kJ/mol, and the binding equilibrium dissociation constants (KD) were 20.3 and 1.69 nM, respectively ( Fig. 1B and 1C) ......
Document: ( Supplementary Data Fig. 1A, Table S1 ), we verified the binding mode of S416 at the ubiquinone-binding site of DHODH that similar to S312. The binding free energies for S312 and S416 were -45.06 and -46.74 kJ/mol, and the binding equilibrium dissociation constants (KD) were 20.3 and 1.69 nM, respectively ( Fig. 1B and 1C) .
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