6HWN
Structure of Thermus thermophilus ClpP in complex with a tripeptide.
Summary for 6HWN
Entry DOI | 10.2210/pdb6hwn/pdb |
Descriptor | ATP-dependent Clp protease proteolytic subunit, Unknown tripeptide, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
Functional Keywords | hydrolase, complex, activator |
Biological source | Thermus thermophilus More |
Total number of polymer chains | 14 |
Total formula weight | 163059.08 |
Authors | Felix, J.,Schanda, P.,Fraga, H.,Morlot, C. (deposition date: 2018-10-12, release date: 2019-09-18, Last modification date: 2024-01-24) |
Primary citation | Felix, J.,Weinhaupl, K.,Chipot, C.,Dehez, F.,Hessel, A.,Gauto, D.F.,Morlot, C.,Abian, O.,Gutsche, I.,Velazquez-Campoy, A.,Schanda, P.,Fraga, H. Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors. Sci Adv, 5:eaaw3818-eaaw3818, 2019 Cited by PubMed: 31517045DOI: 10.1126/sciadv.aaw3818 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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