6WEY
High-resolution structure of the SARS-CoV-2 NSP3 Macro X domain
Summary for 6WEY
| Entry DOI | 10.2210/pdb6wey/pdb |
| Related | 6VXS |
| Descriptor | Non-structural protein 3 (2 entities in total) |
| Functional Keywords | macro domain, adp-ribose-binding, sars-cov-2, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2, COVID-19 virus) |
| Total number of polymer chains | 1 |
| Total formula weight | 18494.11 |
| Authors | Vuksanovic, N.,Silvaggi, N.R. (deposition date: 2020-04-03, release date: 2020-04-29, Last modification date: 2023-10-18) |
| Primary citation | Frick, D.N.,Virdi, R.S.,Vuksanovic, N.,Dahal, N.,Silvaggi, N.R. Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3. Biochemistry, 59:2608-2615, 2020 Cited by PubMed Abstract: The virus that causes COVID-19, SARS-CoV-2, has a large RNA genome that encodes numerous proteins that might be targets for antiviral drugs. Some of these proteins, such as the RNA-dependent RNA polymerase, helicase, and main protease, are well conserved between SARS-CoV-2 and the original SARS virus, but several others are not. This study examines one of the proteins encoded by SARS-CoV-2 that is most different, a macrodomain of nonstructural protein 3 (nsp3). Although 26% of the amino acids in this SARS-CoV-2 macrodomain differ from those observed in other coronaviruses, biochemical and structural data reveal that the protein retains the ability to bind ADP-ribose, which is an important characteristic of beta coronaviruses and a potential therapeutic target. PubMed: 32578982DOI: 10.1021/acs.biochem.0c00309 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.95 Å) |
Structure validation
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