Author: Wanchao Yin; Chunyou Mao; Xiaodong Luan; Dan-Dan Shen; Qingya Shen; Haixia Su; Xiaoxi Wang; Fulai Zhou; Wenfeng Zhao; Minqi Gao; Shenghai Chang; Yuan-Chao Xie; Guanghui Tian; He-Wei Jiang; Sheng-Ce Tao; Jingshan Shen; Yi Jiang; Hualiang Jiang; Yechun Xu; Shuyang Zhang; Yan Zhang; H. Eric Xu
Title: Structural Basis for the Inhibition of the RNA-Dependent RNA Polymerase from SARS-CoV-2 by Remdesivir Document date: 2020_4_9
ID: 7v7pzclb_10
Snippet: The RMP position is at the center of the catalytic active site ( Figure 5 ). The adenosine analog of RMP forms base-stacking interactions with upstream base from the primer strand and two hydrogen bonds with the uridine base from the template strand ( Figure 5B and Figure S5 ). In addition, adenosine analog of RMP also forms interactions with side chains from K545 and R555. Near the bound RMP are two magnesium ions and a pyrophosphate. Both magne.....
Document: The RMP position is at the center of the catalytic active site ( Figure 5 ). The adenosine analog of RMP forms base-stacking interactions with upstream base from the primer strand and two hydrogen bonds with the uridine base from the template strand ( Figure 5B and Figure S5 ). In addition, adenosine analog of RMP also forms interactions with side chains from K545 and R555. Near the bound RMP are two magnesium ions and a pyrophosphate. Both magnesium ions interact with phosphate diester backbone and they are part of catalytic active site. The pyrophosphate is at the gate of nucleotide entry channel to the active site and may block the entry of nucleotide triphosphate (NTP) to the active side ( Figure 5A and 5B).
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