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-Structure paper
Title | Extensive targeting of chemical space at the prime side of ketoamide inhibitors of rhomboid proteases by branched substituents empowers their selectivity and potency. |
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Journal, issue, pages | Eur. J. Med. Chem., Vol. 275, Page 116606-116606, Year 2024 |
Publish date | Jul 4, 2022 (structure data deposition date) |
![]() | Bach, K. / Dohnalek, J. / Skerlova, J. / Kuzmik, J. / Polachova, E. / Stanchev, S. / Majer, P. / Fanfrlik, J. / Pecina, A. / Rezac, J. ...Bach, K. / Dohnalek, J. / Skerlova, J. / Kuzmik, J. / Polachova, E. / Stanchev, S. / Majer, P. / Fanfrlik, J. / Pecina, A. / Rezac, J. / Lepsik, M. / Borshchevskiy, V. / Polovinkin, V. / Strisovsky, K. |
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Methods | X-ray diffraction |
Resolution | 2.4 Å |
Structure data | ![]() PDB-8ab5: |
Chemicals | ![]() ChemComp-HOH: |
Source |
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![]() | HYDROLASE / rhomboid / protease / GlpG / ketoamide / inhibitor |