EC Number   |
|---|
   1.13.11.47 | crystallized by the vapour-diffusion method, giving hexagonal bipyramid crystals belonging to space group P6122. Selenomethionine-containing native QDO is prepared and crystallized under identical conditions |
| 1.13.11.47 | HOD mutant C69S/H251A in complex with its natural 1-H-3-hydroxy-4-oxoquinaldine substrate, its N-acetylanthranilate reaction product, and chloride as dioxygen mimic, X-ray diffraction structure determination and analysis at 2.1 A resolution |
| 1.13.11.47 | mutations H251A and D126A have a minor effect on substrate positioning. Both His-251 and Asp-126 are essential for the proton transfer driving force of the initial reaction |
| 1.13.11.47 | QDO in complex with its natural 1-H-3-hydroxy-4-oxoquinoline substrate, its N-formylanthranilate reaction product, and chloride as dioxygen mimic, X-ray diffraction structure determination and analysis at 2.6 A resolution |
| 1.13.11.47 | random-acceleration molecular dynamics study. Gates for expulsion of O2 from the protein, which can also be taken as gates for O2 uptake, are found throughout almost the whole external surface of the protein, alongside a variety of binding pockets for O2 . The most exploited gates and binding pockets do not correspond to the single gate and binding pocket proposed from the examination of the static model from X-ray diffraction analysis |
