5DP8
Crystal Structure of EV71 3C Proteinase in complex with compound 8
Summary for 5DP8
| Entry DOI | 10.2210/pdb5dp8/pdb |
| Related | 5DP3 5DP4 5DP5 5DP6 5DP7 5DP9 5DPA |
| Descriptor | 3C proteinase, ethyl (2Z,4S)-4-[(N-{[(2-cyclopropylethyl)amino](oxo)acetyl}-L-phenylalanyl)amino]-5-[(3S)-2-oxopyrrolidin-3-yl]pent-2-enoate (3 entities in total) |
| Functional Keywords | hand, foot and mouth disease, 3c proteinase, peptidomimetics, drug design, rupintrivir, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Enterovirus A71 |
| Cellular location | Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Virion : A9XG43 |
| Total number of polymer chains | 1 |
| Total formula weight | 21904.08 |
| Authors | |
| Primary citation | Wu, C.,Zhang, L.,Li, P.,Cai, Q.,Peng, X.,Yin, K.,Chen, X.,Ren, H.,Zhong, S.,Weng, Y.,Guan, Y.,Chen, S.,Wu, J.,Li, J.,Lin, T. Fragment-wise design of inhibitors to 3C proteinase from enterovirus 71 Biochim.Biophys.Acta, 1860:1299-1307, 2016 Cited by PubMed Abstract: Enterovirus 71 (EV71) is a causative agent of hand, foot and mouth disease (HFMD), which can spread its infection to central nervous and other systems with severe consequence. A key factor in the replication of EV71 is its 3C proteinase (3C(pro)), a significant drug target. Peptidomimetics were employed as inhibitors of this enzyme for developing antivirals. However, the peptide bonds in these peptidomimetics are a source of low bioavailability due to their susceptibility to protease digestion. To produce non-peptidomimetic inhibitors by replacing these peptide bonds, it would be important to gain better understanding on the contribution of each component to the interaction and potency. PubMed: 26987809DOI: 10.1016/j.bbagen.2016.03.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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