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: 23615903 DOI: 10.1074/jbc.M112.443390 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.16 Å)

Structure validation