3M3T
SARS-CoV main protease monomeric Arg298Ala mutant with N-terminal additional residues (Gly-Ser)
Summary for 3M3T
Entry DOI | 10.2210/pdb3m3t/pdb |
Related | 2QCY 3M3S 3M3V |
Descriptor | 3C-like proteinase (2 entities in total) |
Functional Keywords | sars protease arg298ala monomeric, hydrolase |
Biological source | SARS coronavirus (SARS-CoV) |
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): P0C6U8 |
Total number of polymer chains | 1 |
Total formula weight | 33934.64 |
Authors | Shi, J.H.,Song, J.X. (deposition date: 2010-03-10, release date: 2011-03-23, Last modification date: 2023-11-01) |
Primary citation | Shi, J.H.,Song, J.X. SARS-CoV main protease with N-terminal extension regulated by mutation on C-terminal domain To be Published, |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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