5KGX
HIV1 catalytic core domain in complex with an inhibitor (2~{S})-2-[3-(3,4-dihydro-2~{H}-chromen-6-yl)-1-methyl-indol-2-yl]-2-[(2-methylpropan-2-yl)oxy]ethanoic acid
Summary for 5KGX
| Entry DOI | 10.2210/pdb5kgx/pdb |
| Related | 5KGW |
| Descriptor | Integrase, (2S)-tert-butoxy[3-(3,4-dihydro-2H-1-benzopyran-6-yl)-1-methyl-1H-indol-2-yl]acetic acid, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | integrase allini, nucleic acid binding, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 18672.01 |
| Authors | Feng, L.,Kobe, M.,Kvaratskhelia, M. (deposition date: 2016-06-13, release date: 2016-10-19, Last modification date: 2024-11-13) |
| Primary citation | Patel, P.A.,Kvaratskhelia, N.,Mansour, Y.,Antwi, J.,Feng, L.,Koneru, P.,Kobe, M.J.,Jena, N.,Shi, G.,Mohamed, M.S.,Li, C.,Kessl, J.J.,Fuchs, J.R. Indole-based allosteric inhibitors of HIV-1 integrase. Bioorg.Med.Chem.Lett., 26:4748-4752, 2016 Cited by PubMed Abstract: Employing a scaffold hopping approach, a series of allosteric HIV-1 integrase (IN) inhibitors (ALLINIs) have been synthesized based on an indole scaffold. These compounds incorporate the key elements utilized in quinoline-based ALLINIs for binding to the IN dimer interface at the principal LEDGF/p75 binding pocket. The most potent of these compounds displayed good activity in the LEDGF/p75 dependent integration assay (IC50=4.5μM) and, as predicted based on the geometry of the five- versus six-membered ring, retained activity against the A128T IN mutant that confers resistance to many quinoline-based ALLINIs. PubMed: 27568085DOI: 10.1016/j.bmcl.2016.08.037 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.67 Å) |
Structure validation
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