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; PubMed: 26566002; DOI: 10.1002/anie.201507266

Experimental method

X-RAY DIFFRACTION (3 Å)