EC Number |
Reference |
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3.1.26.13 | 2.80 A and 2.04 A resolution crystal structures of inhibitor, beta-thujaplicinol, bound at the RNase H active site of both HIV-1 RT and an isolated RNase H domain. beta-Thujaplicinol chelates two divalent metal ions at the RNase H active site |
710577 |
3.1.26.13 | crystal structure analysis, overview. The pyrimidinol carboxylic acids is successful crystallized with Mn2+ and the isolated HIV RNase H domain |
716995 |
3.1.26.13 | crystal structure of domain swapped Rnase H, overview |
751727 |
3.1.26.13 | determination and analysis of crystal structure of enzyme mutant C280S in complex with inhibitor 6-benzyl-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione, PDB ID 6AOC, hanging drop vapor diffusion method, mixing of 11 mg/ml protein in 10 mM MnCl2, 5 mM tris(2-carboxyethyl)phosphine (TCEP) HCl, 0.5% beta-octylglucoside, and 1 mM 6-benzyl-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione in a 1:1 ratio with crystallization solution containing 15% PEG 3500, 0.1 M sodium potassium phosphate, 5% ethylene glycol, and 0.1 M Tris, pH 6.5, large, blocky crystals grow at 18°C in 2-3 days, molecular replacement using structure PDB ID 4KFB as the initial search model |
750467 |
3.1.26.13 | docking simulation studies. Residue His 539 and two metal ions in the RNase H catalytic center are involved in inhibition by compounds 5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester and 5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester |
693579 |
3.1.26.13 | HIV-1 reverse transcriptase mutant form RT52A in complex with rilpivirine and an RNase H inhibitor XZ462, hanging drop vapor diffusion method, the crystallization solution contains 10% PEG 8000, 50 mM imidazole, pH 6.8, 10 mM spermine, 15 mM MgSO4, and 100 mM (NH4)2SO4, crystals of the RT-rilpivirine (RPV) complex are soaked for 30 min with 2 mM compound XZ462 in the crystallization solution in presence of 15 mM MgSO4, X-ray diffraction structure determination and analysis at 1.51-2.2 A resolution, molecular replacement using the 1.51 A resolution structure of the HIV-1 RT-rilpivirine complex (PDB ID 4G1Q) as template |
751430 |
3.1.26.13 | in complex with substrate, hanging drop vapor diffusion method, using 50 mM Bis-Tris propane-HCl pH 7.0, 10% PEG 8000 (w/v), 100 mM ammonium sulfate, 5% glycerol (v/v), 5% sucrose (w/v) and 20 mM MgCl2 |
730522 |
3.1.26.13 | isolated recombinant RNase H domain, to 2.4 A resolution. The protein folds into a five-stranded mixed beta sheet flanked by an asymmetric distribution of four alpha helices. Two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues. The peptide bond cleaved by HIV-1 protease near the polymerase-RNase H junction of polypeptide p66 is completely inaccessible to solvent in the structure reported here, suggesting that the homodimeric p66-p66 precursor of mature RT is asymmetric with one of the two RNase H domains at least partially unfolded |
701216 |
3.1.26.13 | modeling of the kinetic refolding intermediate using a C-terminal deletion fragment lacking helix E. Like the kinetic intermediate, this variant folds rapidly and shows a decrease in stability |
701113 |
3.1.26.13 | purified p66/p51 HIV-1 reverse transcriptase 52A variant in complex with inhibitors manicol and TMC278, 0.0012 ml of 20 mg/mL protein in 9.2 mM Tris, pH 8.0, 68.7 mM NaCl, 3.6 mM manganese sulfate, 0.7 mM tris(2-carboxyethyl) phosphine, 0.27% w/v, beta-ocytl glucopyranoside, 7% v/v DMSO, 0.9 mM manicol, and 0.7 mM TMC278, mixed with 0.0012 ml of reservoir solution containing 50 mM HEPES pH 7.5, 100 mM ammonium sulfate, 15 mM manganese sulfate, 10 mM spermine, 5 mM TCEP, and 11% w/w PEG 8000, X-ray diffraction structure determination and analysis at 2.7 A resolution, modeling |
715864 |