4DFG
Crystal Structure of Wild-type HIV-1 Protease with Cyclopentyltetrahydro- furanyl Urethanes as P2-ligand, GRL-0249A
Summary for 4DFG
| Entry DOI | 10.2210/pdb4dfg/pdb |
| Related | 2HB3 2IEN 2Z4O 3DJK 3DK1 3H5B 3I6O 3OK9 3ST5 |
| Descriptor | Protease, SODIUM ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | aspartic acid protease, hiv-1 protease inhibitor grl-0249a, cyclopentyltetrahydro- furanyl urethanes p2-ligands, wild-type hiv-1 protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Human immunodeficiency virus type 1 (HIV-1) |
| Cellular location | Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P03367 |
| Total number of polymer chains | 2 |
| Total formula weight | 22302.90 |
| Authors | Wang, Y.-F.,Agniswamy, J.,Weber, I.T. (deposition date: 2012-01-23, release date: 2012-03-21, Last modification date: 2023-09-13) |
| Primary citation | Ghosh, A.K.,Chapsal, B.D.,Steffey, M.,Agniswamy, J.,Wang, Y.F.,Amano, M.,Weber, I.T.,Mitsuya, H. Substituent effects on P2-cyclopentyltetrahydrofuranyl urethanes: Design, synthesis, and X-ray studies of potent HIV-1 protease inhibitors. Bioorg.Med.Chem.Lett., 22:2308-2311, 2012 Cited by PubMed: 22364812DOI: 10.1016/j.bmcl.2012.01.061 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.23 Å) |
Structure validation
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