3MT6
Structure of ClpP from Escherichia coli in complex with ADEP1
Summary for 3MT6
Entry DOI | 10.2210/pdb3mt6/pdb |
Related | 1TYF 1Y7O 1YG6 2FZS 3KTG 3KTH 3KTI 3KTJ 3KTK |
Related PRD ID | PRD_000503 |
Descriptor | ATP-dependent Clp protease proteolytic subunit, ACYLDEPSIPEPTIDE 1, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total) |
Functional Keywords | endopeptidase clp, caseinolytic protease, protease ti, acypdepsipeptide antibiotics, hydrolase-antibiotic complex, hydrolase/antibiotic |
Biological source | Escherichia coli More |
Cellular location | Cytoplasm: P0A6G7 |
Total number of polymer chains | 56 |
Total formula weight | 677085.71 |
Authors | Chung, Y.S. (deposition date: 2010-04-30, release date: 2010-11-03, Last modification date: 2023-11-22) |
Primary citation | Li, D.H.,Chung, Y.S.,Gloyd, M.,Joseph, E.,Ghirlando, R.,Wright, G.D.,Cheng, Y.Q.,Maurizi, M.R.,Guarne, A.,Ortega, J. Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP. Chem.Biol., 17:959-969, 2010 Cited by PubMed: 20851345DOI: 10.1016/j.chembiol.2010.07.008 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.901 Å) |
Structure validation
Download full validation report