EC Number   |
|---|
   1.10.5.1 | - |
| 1.10.5.1 | 2.1 A resolution |
| 1.10.5.1 | crystal structure of quinone reductase 2 in complexes with dopamine and adrenochrome |
| 1.10.5.1 | crystal structure of the enzyme in complex with resveratrol. Crystals of the native QR2 and QR2-resveratrol complex all belong to the P2(1)2(1)2(1) space group |
| 1.10.5.1 | purified NQO2 in complex with primaquine and chloroquine, hanging drop vapor diffusion method, against reservoirs containing 0.1 M HEPES, pH 7.5, and 1.3-2.0 M (NH4)2SO4, crystals of NQO2-CQ are soaked in 0.001 ml of reducing-soak solution consisting of 0.1 M HEPES, pH 7.5, 2.0 M (NH4)2SO4, 10 mM 1-(3-sulfonatopropyl)-3-carbamoyl-1,4-dihydropyrimidine and 1 mM chloroquine, X-ray diffraction structure determination and analysis at 1.2-1.4 A resolution |
| 1.10.5.1 | purified recombinant enzyme, hanging-drop, vapor-diffusion method, mixing of 0.001 ml of 4 mg/ml protein solution with 0.001 ml of reservoir solution containing 1.3-1.7 M ammonium sulfate, 0.1 M Bis-Tris buffer, pH 6.0-7.0, 0.1 M NaCl, 5 mM DTT, 0.012 mM FAD, and resveratrol, complexed with different inhibitors, X-ray diffraction structure determination and analysis at resolutions of 1.40-1.63 A |
| 1.10.5.1 | the crystal structure of melatonin and 2-iodomelatonin in complex with quinone reductase 2 provide a detailed description of the enzyme active site that can now be utilized in the design of new and potent inhibitors of the enzyme, hanging-drop vapour-diffusion method |
| 1.10.5.1 | X-ray crystal structure of NQO2 bound to imatinib to 1.75 A resolution. The X-ray structure provides an explanation for the binding specificity of NQO2 for imatinib and nilotinib, as well as for the effects of mutation of the reported phosphorylation sites on NQO2 |
| 1.10.5.1 | X-ray crystallography studies of QR2 in complex with 6-methoxy-9-methyl-[1,3]dioxolo[4,5-h]quinolin-8(9H)-one |
