7BF6
Crystal structure of SARS-CoV-2 macrodomain in complex with remdesivir metabolite GS-441524
Summary for 7BF6
| Entry DOI | 10.2210/pdb7bf6/pdb |
| Descriptor | Papain-like protease nsp3, (2~{R},3~{R},4~{S},5~{R})-2-(4-azanylpyrrolo[2,1-f][1,2,4]triazin-7-yl)-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolane-2-carbonitrile, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | nsp3, macrodomain, sars-cov-2, remdesivir, gs-441524, covid-19, structural genomics, structural genomics consortium, sgc, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 |
| Total number of polymer chains | 3 |
| Total formula weight | 57213.25 |
| Authors | Ni, X.,Knapp, S.,Chaikuad, A.,Structural Genomics Consortium,Structural Genomics Consortium (SGC) (deposition date: 2020-12-31, release date: 2021-01-13, Last modification date: 2024-01-31) |
| Primary citation | Ni, X.,Schroder, M.,Olieric, V.,Sharpe, M.E.,Hernandez-Olmos, V.,Proschak, E.,Merk, D.,Knapp, S.,Chaikuad, A. Structural Insights into Plasticity and Discovery of Remdesivir Metabolite GS-441524 Binding in SARS-CoV-2 Macrodomain. Acs Med.Chem.Lett., 12:603-609, 2021 Cited by PubMed Abstract: The nsP3 macrodomain is a conserved protein interaction module that plays essential regulatory roles in the host immune response by recognizing and removing posttranslational ADP-ribosylation sites during SARS-CoV-2 infection. Thus targeting this protein domain may offer a therapeutic strategy to combat current and future virus pandemics. To assist inhibitor development efforts, we report here a comprehensive set of macrodomain crystal structures complexed with diverse naturally occurring nucleotides, small molecules, and nucleotide analogues including GS-441524 and its phosphorylated analogue, active metabolites of remdesivir. The presented data strengthen our understanding of the SARS-CoV-2 macrodomain structural plasticity and provide chemical starting points for future inhibitor development. PubMed: 33850605DOI: 10.1021/acsmedchemlett.0c00684 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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