7UVM

Crystal structure of human ClpP protease in complex with TR-27

Summary for 7UVM

Entry DOI	10.2210/pdb7uvm/pdb
Descriptor	ATP-dependent Clp protease proteolytic subunit, mitochondrial, (10R)-4-[(4-chlorophenyl)methyl]-7-[(3-ethynylphenyl)methyl]-2,4,6,7,8,9-hexahydroimidazo[1,2-a]pyrido[3,4-e]pyrimidin-5(1H)-one (3 entities in total)
Functional Keywords	agonist, protease, degradation, apoptosis, hydrolase, hydrolase-agonist complex, hydrolase/agonist
Biological source	Homo sapiens (human)
Total number of polymer chains	7
Total formula weight	172275.63
Authors	Mabanglo, M.F.,Houry, W.A. (deposition date: 2022-05-02, release date: 2023-01-11, Last modification date: 2023-10-25)
Primary citation	Mabanglo, M.F.,Wong, K.S.,Barghash, M.M.,Leung, E.,Chuang, S.H.W.,Ardalan, A.,Majaesic, E.M.,Wong, C.J.,Zhang, S.,Lang, H.,Karanewsky, D.S.,Iwanowicz, A.A.,Graves, L.M.,Iwanowicz, E.J.,Gingras, A.C.,Houry, W.A. Potent ClpP agonists with anticancer properties bind with improved structural complementarity and alter the mitochondrial N-terminome. Structure, 31:185-, 2023 Cited by PubMed: 36586405 DOI: 10.1016/j.str.2022.12.002 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.19 Å)

Structure validation