6ZLR
Soaking competent crystal form of the SARS-CoV-2 Receptor Binding Domain (RBD):CR3022 complex.
This is a non-PDB format compatible entry.
Summary for 6ZLR
| Entry DOI | 10.2210/pdb6zlr/pdb |
| Descriptor | Spike glycoprotein, CR3022 FAB HEAVY CHAIN, CR3022 FAB LIGHT CHAIN, ... (4 entities in total) |
| Functional Keywords | sars-cov-2, viral protein complex, antibody, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) More |
| Total number of polymer chains | 9 |
| Total formula weight | 222446.82 |
| Authors | de Nicola, G.F.,Nichols, C.E. (deposition date: 2020-07-01, release date: 2020-12-23, Last modification date: 2024-10-23) |
| Primary citation | Nichols, C.,Ng, J.,Keshu, A.,Fraternali, F.,De Nicola, G.F. A New Crystal Form of the SARS-CoV-2 Receptor Binding Domain: CR3022 Complex-An Ideal Target for In-Crystal Fragment Screening of the ACE2 Binding Site Surface. Front Pharmacol, 11:615211-615211, 2020 Cited by PubMed Abstract: In-crystal fragment screening is a powerful tool to chemically probe the surfaces used by proteins to interact, and identify the chemical space worth exploring to design protein-protein inhibitors. A crucial prerequisite is the identification of a crystal form where the target area is exposed and accessible to be probed by fragments. Here we report a crystal form of the SARS-CoV-2 Receptor Binding Domain in complex with the CR3022 antibody where the ACE2 binding site on the Receptor Binding Domain is exposed and accessible. This crystal form of the complex is a valuable tool to develop antiviral molecules that could act by blocking the virus entry in cells. PubMed: 33381049DOI: 10.3389/fphar.2020.615211 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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