3HYF
Crystal structure of HIV-1 RNase H p15 with engineered E. coli loop and active site inhibitor
Summary for 3HYF
| Entry DOI | 10.2210/pdb3hyf/pdb |
| Descriptor | Reverse transcriptase/RNaseH, MANGANESE (II) ION, ACETATE ION, ... (6 entities in total) |
| Functional Keywords | rnase h, hiv-1, hydrolase, di-valent metal nucleic acid cleavage mechanism, di-valent metal coordination, aspartyl protease, dna integration, dna recombination, endonuclease, multifunctional enzyme, nuclease, nucleotidyltransferase, protease, rna-directed dna polymerase, transferase, magnesium, metal-binding |
| Biological source | Human immunodeficiency virus 1 More |
| Total number of polymer chains | 1 |
| Total formula weight | 17589.68 |
| Authors | Lansdon, E.B.,Kirschberg, T.A. (deposition date: 2009-06-22, release date: 2009-10-20, Last modification date: 2024-03-13) |
| Primary citation | Kirschberg, T.A.,Balakrishnan, M.,Squires, N.H.,Barnes, T.,Brendza, K.M.,Chen, X.,Eisenberg, E.J.,Jin, W.,Kutty, N.,Leavitt, S.,Liclican, A.,Liu, Q.,Liu, X.,Mak, J.,Perry, J.K.,Wang, M.,Watkins, W.J.,Lansdon, E.B. RNase H active site inhibitors of human immunodeficiency virus type 1 reverse transcriptase: design, biochemical activity, and structural information. J.Med.Chem., 52:5781-5784, 2009 Cited by PubMed Abstract: Pyrimidinol carboxylic acids were designed as inhibitors of HIV-1 RNase H function. These molecules can coordinate to two divalent metal ions in the RNase H active site. Inhibition of enzymatic activity was measured in a biochemical assay, but no antiviral effect was observed. Binding was demonstrated via a solid state structure of the isolated p15-Ec domain of HIV-1 RT showing inhibitor and two Mn(II) ions bound to the RNase H active site. PubMed: 19791799DOI: 10.1021/jm900597q PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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