6BBA
Crystal structure of human mitochondrial ClpP complex with acyldepsipeptide ADEP-28
Summary for 6BBA
Entry DOI | 10.2210/pdb6bba/pdb |
Descriptor | ATP-dependent Clp protease proteolytic subunit, mitochondrial, Acyldepsipeptide ADEP-28 (3 entities in total) |
Functional Keywords | protease, proteostasis, protein quality control, mitochondria, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 14 |
Total formula weight | 174893.57 |
Authors | Mabanglo, M.F.,Houry, W.A. (deposition date: 2017-10-17, release date: 2018-07-11, Last modification date: 2023-11-15) |
Primary citation | Wong, K.S.,Mabanglo, M.F.,Seraphim, T.V.,Mollica, A.,Mao, Y.Q.,Rizzolo, K.,Leung, E.,Moutaoufik, M.T.,Hoell, L.,Phanse, S.,Goodreid, J.,Barbosa, L.R.S.,Ramos, C.H.I.,Babu, M.,Mennella, V.,Batey, R.A.,Schimmer, A.D.,Houry, W.A. Acyldepsipeptide Analogs Dysregulate Human Mitochondrial ClpP Protease Activity and Cause Apoptotic Cell Death. Cell Chem Biol, 25:1017-1030.e9, 2018 Cited by PubMed: 30126533DOI: 10.1016/j.chembiol.2018.05.014 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.796 Å) |
Structure validation
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