2X78
Human foamy virus integrase - catalytic core.
Summary for 2X78
| Entry DOI | 10.2210/pdb2x78/pdb |
| Related | 2X6N 2X6S 2X74 |
| Descriptor | INTEGRASE (2 entities in total) |
| Functional Keywords | viral protein, retroviral integrase, dna-directed dna polymerase, nucleotidyltransferase, dna integration, aspartyl protease, dna recombination, transferase, nuclease, hydrolase |
| Biological source | HUMAN SPUMARETROVIRUS |
| Cellular location | Integrase: Virion (Potential). Protease/Reverse transcriptase/ribonuclease H: Host nucleus (By similarity): P14350 |
| Total number of polymer chains | 3 |
| Total formula weight | 67571.06 |
| Authors | Rety, S.,Delelis, O.,Rezabkova, L.,Dubanchet, B.,Legrand, P.,Silhan, J.,Lewit-Bentley, A. (deposition date: 2010-02-24, release date: 2010-08-11, Last modification date: 2023-12-20) |
| Primary citation | Rety, S.,Rezabkova, L.,Dubanchet, B.,Silhan, J.,Legrand, P.,Lewit-Bentley, A. Structural Studies of the Catalytic Core of the Primate Foamy Virus (Pfv-1) Integrase Acta Crystallogr.,Sect.F, 66:881-, 2010 Cited by PubMed Abstract: Retroviral integrases are vital enzymes in the viral life cycle and thus are important targets for antiretroviral drugs. The structure of the catalytic core domain of the integrase from human foamy virus, which is related to HIV-1, has been solved. The structure of the protein is presented in two different crystal forms, each containing several molecules in the asymmetric unit, with and without the essential manganese or magnesium ion, and the structures are compared in detail. This allows regions of high structural variability to be pinpointed, as well as the effect of divalent cations on the conformation of the catalytic site. PubMed: 20693659DOI: 10.1107/S1744309110022852 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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