8DLA

ClpP2 from Chlamydia trachomatis bound by MAS1-12

Summary for 8DLA

Entry DOI	10.2210/pdb8dla/pdb
Descriptor	ATP-dependent Clp protease proteolytic subunit 2, 1-{4-[(4-chlorophenyl)methyl]piperazin-1-yl}-2-methyl-2-[5-(trifluoromethyl)pyridine-2-sulfonyl]propan-1-one, SODIUM ION, ... (5 entities in total)
Functional Keywords	protease, chlamydia trachomatis, hydrolase, hydrolase-inhibitor complex, hydrolase/inhibitor
Biological source	Chlamydia trachomatis
Total number of polymer chains	14
Total formula weight	312492.47
Authors	Azadmanesh, J.,Struble, L.R.,Seleem, M.A.,Ouellette, S.,Conda-Sheridan, M.,Borgstahl, G.E.O. (deposition date: 2022-07-07, release date: 2023-08-09, Last modification date: 2024-01-24)
Primary citation	Azadmanesh, J.,Seleem, M.A.,Struble, L.,Wood, N.A.,Fisher, D.J.,Lovelace, J.J.,Artigues, A.,Fenton, A.W.,Borgstahl, G.E.O.,Ouellette, S.P.,Conda-Sheridan, M. The structure of caseinolytic protease subunit ClpP2 reveals a functional model of the caseinolytic protease system from Chlamydia trachomatis. J.Biol.Chem., 299:102762-102762, 2023 Cited by PubMed: 36463962 DOI: 10.1016/j.jbc.2022.102762 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.66 Å)

Structure validation