3DCR
X-ray structure of HIV-1 protease and hydrated form of ketomethylene isostere inhibitor
Summary for 3DCR
| Entry DOI | 10.2210/pdb3dcr/pdb |
| Related | 3DCK |
| Related PRD ID | PRD_001037 |
| Descriptor | Chemical analogue HIV-1 protease, N~2~-[(2R,5S)-5-({(2S,3S)-2-[(N-acetyl-L-threonyl)amino]-3-methylpent-4-enoyl}amino)-2-butyl-4,4-dihydroxynonanoyl]-L-glutaminyl-L-argininamide (3 entities in total) |
| Functional Keywords | hiv-1 protease, homodimer, beta-turn, beta-strand, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Total number of polymer chains | 2 |
| Total formula weight | 22322.24 |
| Authors | Torbeev, V.Y.,Mandal, K.,Terechko, V.A.,Kent, S.B.H. (deposition date: 2008-06-04, release date: 2008-08-19, Last modification date: 2023-11-15) |
| Primary citation | Torbeev, V.Y.,Mandal, K.,Terechko, V.A.,Kent, S.B.H. Crystal structure of chemically synthesized HIV-1 protease and a ketomethylene isostere inhibitor based on the p2/NC cleavage site Bioorg.Med.Chem.Lett., 18:4554-4557, 2008 Cited by PubMed Abstract: Here we report the X-ray structures of chemically synthesized HIV-1 protease and the inactive [D25N]HIV-1 protease complexed with the ketomethylene isostere inhibitor Ac-Thr-Ile-Nle psi[CO-CH(2)]Nle-Gln-Arg.amide at 1.4 and 1.8A resolution, respectively. In complex with the active enzyme, the keto-group was found to be converted into the hydrated gem-diol, while the structure of the complex with the inactive D25N enzyme revealed an intact keto-group. These data support the general acid-general base mechanism for HIV-1 protease catalysis. PubMed: 18657969DOI: 10.1016/j.bmcl.2008.07.039 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
Download full validation report
