5DL1
ClpP from Staphylococcus aureus in complex with AV145
Summary for 5DL1
Entry DOI | 10.2210/pdb5dl1/pdb |
Related | 3V5E |
Descriptor | ATP-dependent Clp protease proteolytic subunit, 1-(propan-2-yl)-N-{[2-(thiophen-2-yl)-1,3-oxazol-4-yl]methyl}-1H-pyrazolo[3,4-b]pyridine-5-carboxamide (2 entities in total) |
Functional Keywords | hydrolase-hydrolase inhibitor complex, caseinolytic protease, allosteric regulation, binding analysis, hydrolase |
Biological source | Staphylococcus aureus |
Total number of polymer chains | 14 |
Total formula weight | 306655.38 |
Authors | Vielberg, M.-T.,Groll, M. (deposition date: 2015-09-04, release date: 2015-11-25, Last modification date: 2024-01-10) |
Primary citation | Pahl, A.,Lakemeyer, M.,Vielberg, M.T.,Hackl, M.W.,Vomacka, J.,Korotkov, V.S.,Stein, M.L.,Fetzer, C.,Lorenz-Baath, K.,Richter, K.,Waldmann, H.,Groll, M.,Sieber, S.A. Reversible Inhibitors Arrest ClpP in a Defined Conformational State that Can Be Revoked by ClpX Association. Angew.Chem.Int.Ed.Engl., 54:15892-15896, 2015 Cited by PubMed: 26566002DOI: 10.1002/anie.201507266 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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