Summary for 2C3S
| Entry DOI | 10.2210/pdb2c3s/pdb |
| Related | 1O5S 1P76 1P9T 1PA5 1PUK 1Q1X 1UJ1 1UK2 1UK3 1UK4 1UW7 1WOF 2AMD 2AMQ 2BX3 2BX4 2D2D |
| Descriptor | SARS COV 3C-LIKE PROTEINASE (2 entities in total) |
| Functional Keywords | sars cov, 3c-like protease, main protease, hydrolase |
| Biological source | SARS CORONAVIRUS |
| Cellular location | Non-structural protein 3: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 4: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 6: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 7: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 8: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 9: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 10: Host cytoplasm, host perinuclear region (By similarity). Helicase: Host endoplasmic reticulum-Golgi intermediate compartment (Potential). Uridylate-specific endoribonuclease: Host cytoplasm, host perinuclear region (By similarity): P59641 |
| Total number of polymer chains | 1 |
| Total formula weight | 33876.64 |
| Authors | Xu, T.,Ooi, A.,Lee, H.-C.,Lescar, J. (deposition date: 2005-10-12, release date: 2005-10-18, Last modification date: 2023-12-13) |
| Primary citation | Xu, T.,Ooi, A.,Lee, H.-C.,Wilmouth, R.,Liu, D.X.,Lescar, J. Structure of the Sars Coronavirus Main Proteinase as an Active C2 Crystallographic Dimer. Acta Crystallogr.,Sect.F, 61:964-, 2005 Cited by PubMed Abstract: The 34 kDa main proteinase (Mpro) from the severe acute respiratory syndrome coronavirus (SARS-CoV) plays an important role in the virus life cycle through the specific processing of viral polyproteins. As such, SARS-CoV Mpro is a key target for the identification of specific inhibitors directed against the SARS virus. With a view to facilitating the development of such compounds, crystals were obtained of the enzyme at pH 6.5 in the orthorhombic space group P2(1)2(1)2 that diffract to a resolution of 1.9 A. These crystals contain one monomer per asymmetric unit and the biologically active dimer is generated via the crystallographic twofold axis. The conformation of the catalytic site indicates that the enzyme is active in the crystalline form and thus suitable for structure-based inhibition studies. PubMed: 16511208DOI: 10.1107/S1744309105033257 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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