3KTH
Structure of ClpP from Bacillus subtilis in orthorombic crystal form
Summary for 3KTH
Entry DOI | 10.2210/pdb3kth/pdb |
Related | 3KTG 3KTI 3KTJ 3KTK |
Descriptor | ATP-dependent Clp protease proteolytic subunit (2 entities in total) |
Functional Keywords | hydrolase, atp-binding, nucleotide-binding, protease, serine protease, stress response |
Biological source | Bacillus subtilis |
Cellular location | Cytoplasm (By similarity): P80244 |
Total number of polymer chains | 7 |
Total formula weight | 154302.89 |
Authors | Lee, B.-G.,Brotz-Oesterhelt, H.,Song, H.K. (deposition date: 2009-11-25, release date: 2010-03-23, Last modification date: 2021-11-10) |
Primary citation | Lee, B.-G.,Park, E.Y.,Lee, K.-E.,Jeon, H.,Sung, K.H.,Paulsen, H.,Rubsamen-Schaeff, H.,Brotz-Oesterhelt, H.,Song, H.K. Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism Nat.Struct.Mol.Biol., 17:471-478, 2010 Cited by PubMed: 20305655DOI: 10.1038/nsmb.1787 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report