EC Number   |
Reference |
|---|
   3.4.23.47 | analysis of 19 ligand-bound wild-type enzyme crystal structures, overview. Mutation K57L is experimentally introduced in 8 structures to help the crystallographic process |
754210 |
| 3.4.23.47 | crystallized by hanging drop method in complex with a reduced amide inhibitor, BI-LA-398 |
644058, 644060, 644061, 644062, 644065, 644066 |
| 3.4.23.47 | crystals grown by hanging-drop vapor diffusion method, thin tetragonal prisms, space group P4(1)2(1)2 or P4(3)2(1)2 with a=b=62.6 A and c=115.8 A |
644065 |
| 3.4.23.47 | in complex with inhibitor amprenavir, to 1.5 A resolution, and comparison with HIV-1 protease PR1M |
718370 |
| 3.4.23.47 | molecular dynamics simulations in complerx with inhibitors amprenvir and darunavir |
735264 |
| 3.4.23.47 | monoclinic crystals, vapor diffusion, hanging drops, P2(1) space group with a =36.76 A, b=58.44 A, c= 55.11 A and beta=91.20° |
644062 |
| 3.4.23.47 | Phe-Val-Phe-psi-CH2NH-Leu-Glu-Ile-amide, space group P4(1) or P4(3), unit-cell parameters a=b=55.1 A, c=138.9 A |
644061 |
| 3.4.23.47 | substrate binding pocket structure analysis |
665102 |
