EC Number   |
|---|
   3.4.22.69 | - |
| 3.4.22.69 | 1.8 A X-ray crystal structure of 3Clpro bound to an irreversible inhibitor, an alpha,beta-epoxyketone |
| 3.4.22.69 | complexed with inhibitors TG-0204998 and TG-0205486, sitting drop vapor diffusion method, using 3-6% (w/v) PEG 6000, 4-6% (v/v) DMSO or methyl-2,4-pentanediol, 1 mM dithiothreitol, 0.1 M MES, pH 6.5 |
| 3.4.22.69 | crystal structure of 3CLpro with the C-terminal prosequence and the catalytic-site C145A mutation. Residue Phe at the P3' position [Phe(P3')] is accommodated in the S3' pocket |
| 3.4.22.69 | crystal structure of monomeric mutant enzyme G11A |
| 3.4.22.69 | crystal structures of 3Cpro from CVB3 and 3CLpro from CoV-229E and SARS-CoV in complex with inhibitors are solved |
| 3.4.22.69 | crystallization of free enzyme and the enzyme/peptide aldehyde inhibitor(benzoyl-YYNQ-H) complex by hanging-drop method. The 3CLpro structure (refined to 1.94 A) shows that the protein forms dimers. The monomers are comprised of N-terminal domains I and II, which adopt a chymotrypsin-like fold, and a C-terminal alpha-helical domain III. The catalytic Cys-His dyad is assisted by a complex network of interactions involving a water molecule that mediates polar contacts between the catalytic His and a conserved Asp located in the domain II-III junction and is suitably positioned to stabilize the developing positive charge of the catalytic His in the transition state during catalysis |
| 3.4.22.69 | crystals grown in hanging-drop vapour-diffusion method |
| 3.4.22.69 | crystals of the enzyme in a complex with the inhibitor (S)-2-(([(3S,4aR,8aS)-2-(4-bromobenzoyl)decahydroisoquinolin-3-yl]methyl)amino)-3-(1H-imidazol-4-yl)-propanal are obtained by co-crystallization using sitting-drop vapor diffusion at 4°C and mixing an equal volume of protein-inhibitor complex |
| 3.4.22.69 | enzyme-inhibitor complex, hanging-drop method |
