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: 36463962DOI: 10.1016/j.jbc.2022.102762 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.66 Å) |
Structure validation
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