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: 30126533 DOI: 10.1016/j.chembiol.2018.05.014 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.796 Å)

Structure validation