EC Number   |
|---|
   3.4.21.83 | crystal structure solved at 2.7 A resolution |
| 3.4.21.83 | in complex with the inhibitor antipain and as mercury derivative, to 1.65 and 2.0 A resolution, respectively. OPB comprises two domains, a catalytic and a propeller domain, linked together by a hinge region. Residue E621 plays a critical role in the S1 binding pocket and, along with F603, is largely responsible for the enzyme substrate specificity in P1. In the S2 binding pocket, Y499 is important for substrate stability. Residue E623 forms an inter-domain hydrogen bond |
| 3.4.21.83 | ligand-free open state and inhibitor-bound closed state crystal structures, to 2.4 and 2.85 A resolution, respectively. Peptides over 30 residues cannot fit the enzyme cavity, preventing the complete domain closure required for a key propeller Asp/Glu to fix the catalytic His and Arg in the catalytically competent conformation. This size exclusion mechanism protects larger peptides and proteins from degradation |
| 3.4.21.83 | using the hanging-drop vapour-diffusion technique in 7% (w/v) polyethylene glycol 6000, 1 M LiCl, 0.1 M bis-tris propane pH 7.5. Diffraction data to 2.7 A resolution are collected using synchrotron radiation. The crystals belong to space group P3121 or P3221, with unit-cell parameters a = b = 124.5, c = 249.9 A. A complete data set to 2.7 A is collected using synchrotron radiation |
| 3.4.21.83 | using the hanging-drop vapour-diffusion technique in 7%(w/v) polyethylene glycol 6000, 1 M LiCl, 0.1 M bis-tris propane pH 7.5. Diffraction data to 2.7 A resolution are collected using synchrotron radiation. The crystals belong to space group P3121 or P3221, with unit-cell parameters a = b = 124.5, c = 249.9 A. A complete data set to 2.7 A is collected using synchrotron radiation |
