EC Number   |
|---|
   4.6.1.2 | crystal structure of the ligand-bound adenylyl cyclase (resulting from the point mutations E497K/C566D) domain at 2.25 A reveals the mechanistic basis for the change from cGMP to cAMP production |
| 4.6.1.2 | H-NOX domain of Tar4H, residues form hydrogen bonds to the heme group, tyrosine at position 140 is critical in discriminating between NO and O2 |
| 4.6.1.2 | homology modeling of the catalytic domain in inactive or active conformations based on PDB entries 2WZ1, 3ET6, 1CJU and molecular dynamics simulations reveals presence of potential high-affinity binding site on the active structure. The site is located between the pseudo-symmetric and the catalytic site just over the loop beta2-beta3 and does not overlap with the forskolin binding site on adenylate cyclases |
| 4.6.1.2 | isolated dimeric and inactive catalytic domain, X-ray diffraction structure determination and analysis at 2.55 A resolution |
| 4.6.1.2 | sitting drop vapor diffusion method, using 0.05 M KH2PO4 and 20% (w/v) PEG 8000 |
| 4.6.1.2 | sitting drop vapor diffusion method, using 0.1 M Bis-Tris pH 7.0, and 0.7 M ammonium sulfate |
| 4.6.1.2 | sitting drop vapor diffusion method, using 1.4-1.6 M ammonium sulfate, 50 mM sodium cacodylate (pH 5.5-6.5) and 15 mM magnesium acetate tetrahydrate |
| 4.6.1.2 | sitting drop vapor diffusion method, using 20% (w/v) PEG3350, 50 mM HEPES (pH 7.0), and 1% (w/v) tryptone |
| 4.6.1.2 | to 1.77 A and 2.5 A resolution, N-terminal heme domain and C-terminal catalytic domain |
