4GVM
HIV-1 Integrase Catalytic Core Domain A128T Mutant Complexed with Allosteric Inhibitor
Summary for 4GVM
Entry DOI | 10.2210/pdb4gvm/pdb |
Descriptor | Gag-Pol polyprotein, ARSENIC, (2S)-[6-bromo-4-(4-chlorophenyl)-2-methylquinolin-3-yl](tert-butoxy)ethanoic acid, ... (4 entities in total) |
Functional Keywords | integrase, ccd, dde motif, dimer interface, allosteric inhibitor, drug resistance, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE) (HIV-1) |
Cellular location | Gag-Pol polyprotein: Host cell membrane; Lipid-anchor . Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P12497 |
Total number of polymer chains | 1 |
Total formula weight | 18555.12 |
Authors | Feng, L.,Kvaratskhelia, M. (deposition date: 2012-08-30, release date: 2013-05-01, Last modification date: 2024-02-28) |
Primary citation | Feng, L.,Sharma, A.,Slaughter, A.,Jena, N.,Koh, Y.,Shkriabai, N.,Larue, R.C.,Patel, P.A.,Mitsuya, H.,Kessl, J.J.,Engelman, A.,Fuchs, J.R.,Kvaratskhelia, M. The A128T Resistance Mutation Reveals Aberrant Protein Multimerization as the Primary Mechanism of Action of Allosteric HIV-1 Integrase Inhibitors. J.Biol.Chem., 288:15813-15820, 2013 Cited by PubMed: 23615903DOI: 10.1074/jbc.M112.443390 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.16 Å) |
Structure validation
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