EC Number   |
Reference  |
|---|
   3.6.1.17 | sitting-drop vapour diffusion, crystals diffract to a minimum d-spacing of 2 A and belong to either space group C222 or C222(1) |
654817 |
| 3.6.1.17 | structure determined by NMR spectroscopy |
669427 |
| 3.6.1.17 | free and ATP-bound enzyme, hanging drop vapor diffusion method, using 0.1 M Tris-HCl pH 7.6, 29% (w/v) PEG 3350, and 0.75 M NaCl (free enzyme) or 1 ml 0.1 M Tris-HCl pH 8.8, 25% (w/v) PEG 3350, and 0.2 M NaCl (ATP-bound enzyme) |
710715 |
| 3.6.1.17 | structure of wild-type and E58A mutant human Ap4A hydrolase, to 2.7 and 2.1 A resolution, respectively. Similar to the canonical Nudix fold, human Ap4A hydrolase shows the common alphabetaalpha-sandwich architecture. Two sulfate ions and one diphosphate coordinated with some conserved residues are observed in the active cleft |
733257 |
| 3.6.1.17 | structures of both apo- and ligand-bound CT771, to 2.6 A and 1.9 A resolution, respectively. The structure shows a alphabetaalpha-sandwich motif with many conserved elements lining the putative Nudix active site |
733346 |
