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7BV1

Cryo-EM structure of the apo nsp12-nsp7-nsp8 complex

Summary for 7BV1
Entry DOI10.2210/pdb7bv1/pdb
EMDB information30209
DescriptorRNA-directed RNA polymerase, Non-structural protein 8, Non-structural protein 7, ... (4 entities in total)
Functional Keywordssars-cov-2, rna polymerase, apo, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV)
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Total number of polymer chains4
Total formula weight165965.28
Authors
Primary citationYin, W.,Mao, C.,Luan, X.,Shen, D.D.,Shen, Q.,Su, H.,Wang, X.,Zhou, F.,Zhao, W.,Gao, M.,Chang, S.,Xie, Y.C.,Tian, G.,Jiang, H.W.,Tao, S.C.,Shen, J.,Jiang, Y.,Jiang, H.,Xu, Y.,Zhang, S.,Zhang, Y.,Xu, H.E.
Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir.
Science, 368:1499-1504, 2020
Cited by
PubMed Abstract: The pandemic of coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has become a global crisis. Replication of SARS-CoV-2 requires the viral RNA-dependent RNA polymerase (RdRp) enzyme, a target of the antiviral drug remdesivir. Here we report the cryo-electron microscopy structure of the SARS-CoV-2 RdRp, both in the apo form at 2.8-angstrom resolution and in complex with a 50-base template-primer RNA and remdesivir at 2.5-angstrom resolution. The complex structure reveals that the partial double-stranded RNA template is inserted into the central channel of the RdRp, where remdesivir is covalently incorporated into the primer strand at the first replicated base pair, and terminates chain elongation. Our structures provide insights into the mechanism of viral RNA replication and a rational template for drug design to combat the viral infection.
PubMed: 32358203
DOI: 10.1126/science.abc1560
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.8 Å)
Structure validation

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