2A5A
Crystal structure of unbound SARS coronavirus main peptidase in the space group C2
Summary for 2A5A
Entry DOI | 10.2210/pdb2a5a/pdb |
Related | 2A5I 2A5K |
Descriptor | 3C-like peptidase, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | cysteine peptidase, 3c-like, n-finger, chymotrypsin-like fold, long loop, alpha-helical domain, dimer, catalytic dyad, specificity pockets, hydrolase |
Biological source | SARS coronavirus |
Total number of polymer chains | 1 |
Total formula weight | 34009.61 |
Authors | Lee, T.-W.,Cherney, M.M.,Huitema, C.,Liu, J.,James, K.E.,Powers, J.C.,Eltis, L.D.,James, M.N. (deposition date: 2005-06-30, release date: 2005-10-25, Last modification date: 2023-08-23) |
Primary citation | Lee, T.-W.,Cherney, M.M.,Huitema, C.,Liu, J.,James, K.E.,Powers, J.C.,Eltis, L.D.,James, M.N. Crystal Structures of the Main Peptidase from the SARS Coronavirus Inhibited by a Substrate-like Aza-peptide Epoxide J.Mol.Biol., 353:1137-1151, 2005 Cited by PubMed: 16219322DOI: 10.1016/j.jmb.2005.09.004 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.08 Å) |
Structure validation
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