1UJ1
Crystal structure of SARS Coronavirus Main Proteinase (3CLpro)
Summary for 1UJ1
| Entry DOI | 10.2210/pdb1uj1/pdb |
| Descriptor | 3C-like proteinase (2 entities in total) |
| Functional Keywords | anti-parallel b-barrel, anti-parallel a-helices, 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 | 2 |
| Total formula weight | 67753.27 |
| Authors | |
| Primary citation | Yang, H.,Yang, M.,Ding, Y.,Liu, Y.,Lou, Z.,Zhou, Z.,Sun, L.,Mo, L.,Ye, S.,Pang, H.,Gao, G.F.,Anand, K.,Bartlam, M.,Hilgenfeld, R.,Rao, Z. The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor Proc.Natl.Acad.Sci.USA, 100:13190-13195, 2003 Cited by PubMed Abstract: A newly identified severe acute respiratory syndrome coronavirus (SARS-CoV), is the etiological agent responsible for the outbreak of SARS. The SARS-CoV main protease, which is a 33.8-kDa protease (also called the 3C-like protease), plays a pivotal role in mediating viral replication and transcription functions through extensive proteolytic processing of two replicase polyproteins, pp1a (486 kDa) and pp1ab (790 kDa). Here, we report the crystal structures of the SARS-CoV main protease at different pH values and in complex with a specific inhibitor. The protease structure has a fold that can be described as an augmented serine-protease, but with a Cys-His at the active site. This series of crystal structures, which is the first, to our knowledge, of any protein from the SARS virus, reveal substantial pH-dependent conformational changes, and an unexpected mode of inhibitor binding, providing a structural basis for rational drug design. PubMed: 14585926DOI: 10.1073/pnas.1835675100 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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