EC Number   |
Reference  |
|---|
   3.4.22.71 | 1.6 A resolution. Space group P2(1) with cell dimension of a = 40.47 A, b = 64.6 A, c = 42.96 A, alpha = 105.77°, beta = 105.77°, gamma = 90° |
666932 |
| 3.4.22.71 | 2.0 A resolution. Space group P2(1)2(1)2(1) with cell dimension of a = 71.208 A, b = 104.367 A, c = 58.087 A, alpha = beta = gamma = 90° |
666932 |
| 3.4.22.71 | hanging or sitting drop vapor diffusion method, using 10% (w/v) polyethylene glycol 3350, 0.2 M Zn(OAc)2, 0.1 M NaOAc, pH 6.2 |
718269 |
| 3.4.22.71 | hanging-drop vapor diffusion method. Crystal structure of SrtB-DELTA-N30 in complex with two active site inhibitors E64 and MTSET, and with the cell wall substrate analog tripleglycine |
647690 |
| 3.4.22.71 | sortase B enzyme in a covalent complex with an analogue of its NPQTN sorting signal substrate, hanging drop vapour diffusion method, micing of 0.150 mMSrtB-NPQT in 10 mM Tris-HCl, pH 7.0, 20 mM NaCl, with reservoir solution containing 2.8 M ammonium sulfate, 70 mM sodium citrate, pH 5.0, X-ray diffraction structure determination and analysis at 2.49 A resolution, molecular replacement method |
732174 |
| 3.4.22.71 | SrtB in complex with aryl (beta-amino)ethyl ketone inhibitors. Analysis of the three-dimensional structure ofBacillusanthracissortaseBwithandwithoutinhibitorprovidesinsights into the mechanism of inhibition |
680796 |
| 3.4.22.71 | structures of SrtB and its inactive mutant at 2.2 A and 1.8 A, respectively. The position of Cys232 found is preferable for the catalytic reaction to occur. Structural comparison with other class B sortases demonstrates that the catalytic site likely converts between two forms. The movement of Cys232 between the two forms may help His136 deprotonate Cys232 to be activated as a thiolate |
752669 |
| 3.4.22.71 | truncated variant with deletion of 26 residues at the N-terminal transmembrane domain |
753652 |
