EC Number   |
|---|
   3.4.22.38 | - |
| 3.4.22.38 | complexed with synthetic inhibitors |
| 3.4.22.38 | crysallized from 20% MPD, 0.1 M Tris, pH 7 and 0.1 M MES, pH 6, crystals were flash frozen in a nitrogen stream after increasing the MPD concentration to aproximately 30% |
| 3.4.22.38 | crystal structure of enzyme-inhibitor complex, inhibitor: N-[1S-(2-phenylethyl)-3-phenylsulfonylallyl]-4-methyl-2R-piperazinyl carbonylaminovaleramide, i.e. APC3328 |
| 3.4.22.38 | hanging drop vapour diffusion method |
| 3.4.22.38 | in complex with NSC13345, sitting drop vapor diffusion method, using 0.2 M ammonium sulfate, pH 5.5, 30% (w/v) PEG-8000 |
| 3.4.22.38 | inhibitor: trans-epoxysuccinyl-L-leucylamido- (4-guanidino)butane, i.e. E-64 |
| 3.4.22.38 | mutant K9E/I171E/Q172S/N190M/K191G/L195K (E-64 inhibited) in complex with the 17000 Da fraction of chondroitin 4-sulfate, hanging drop vapor diffusion method, using 30% (v/v) 2-methyl-2,4-pentanediol, 0.1 M sodium acetate buffer, pH 4.5, and 20 mM CaCl2 |
| 3.4.22.38 | purified and activated, recombinant cathepsin K in complex with chondroitin sulfate in presence or absence of inhibitor E64, which prevents autocatalytic cleavage of cathepsin K, 25 mg/ml enzyme-inhibitor complex of ratio 1:1 in 50 mM sodium acetate buffer, pH 5.5, hanging drop vapor diffusion method, mixing with an equal volume of reservoir solution containing 30% v/v 2-methyl-2,4-pentanediol, 0.1 M sodium acetate buffer, pH 4.5, and 20 mM calcium chloride, macroseeding, X-ray diffraction structure determination and analysis at 1.8 A resolution |
| 3.4.22.38 | the overall organization of the catalytic site, which consists of two domains folds together to give a V-shaped active site cleft configuration. The central helix is the most prominent feature of the left domain, whereas the right domain is mostly dominated by beta-barrel motifs (5-6 strands). The active site lies at the interface between the two domains |
