4ZIP
HIV-1 wild Type protease with GRL-0648A (a isophthalamide-derived P2-Ligand)
Summary for 4ZIP
| Entry DOI | 10.2210/pdb4zip/pdb |
| Related | 2IEN 3OK9 3QAA 4U8W |
| Descriptor | Protease, SODIUM ION, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Human immunodeficiency virus type 1 (HIV-1) |
| Total number of polymer chains | 2 |
| Total formula weight | 22439.63 |
| Authors | Wang, Y.-F.,Agniswamy, J.,Weber, I.T. (deposition date: 2015-04-28, release date: 2015-07-15, Last modification date: 2023-09-27) |
| Primary citation | Ghosh, A.K.,Takayama, J.,Kassekert, L.A.,Ella-Menye, J.R.,Yashchuk, S.,Agniswamy, J.,Wang, Y.F.,Aoki, M.,Amano, M.,Weber, I.T.,Mitsuya, H. Structure-based design, synthesis, X-ray studies, and biological evaluation of novel HIV-1 protease inhibitors containing isophthalamide-derived P2-ligands. Bioorg.Med.Chem.Lett., 25:4903-4909, 2015 Cited by PubMed Abstract: We describe the design, synthesis and biological evaluation of a series of novel HIV-1 protease inhibitors bearing isophthalamide derivatives as the P2-P3 ligands. We have investigated a range of acyclic and heterocyclic amides as the extended P2-P3 ligands. These inhibitors displayed good to excellent HIV-1 protease inhibitory activity. Also, a number of inhibitors showed very good antiviral activity in MT cells. Compound 5n has shown an enzyme Ki of 0.17 nM and antiviral IC50 of 14 nM. An X-ray crystal structure of inhibitor 5o-bound to HIV-1 protease was determined at 1.11Å resolution. This structure revealed important molecular insight into the inhibitor-HIV-1 protease interactions in the active site. PubMed: 26096678DOI: 10.1016/j.bmcl.2015.05.052 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.11 Å) |
Structure validation
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