1Y7O
The structure of Streptococcus pneumoniae A153P ClpP
Summary for 1Y7O
Entry DOI | 10.2210/pdb1y7o/pdb |
Descriptor | ATP-dependent Clp protease proteolytic subunit, CALCIUM ION (3 entities in total) |
Functional Keywords | protease, hydrolase |
Biological source | Streptococcus pneumoniae |
Total number of polymer chains | 7 |
Total formula weight | 170284.73 |
Authors | Kimber, M.S.,Gribun, A.,Ching, R.,Sprangers, R.,Fiebig, K.M.,Houry, W.A. (deposition date: 2004-12-09, release date: 2005-02-08, Last modification date: 2023-11-15) |
Primary citation | Gribun, A.,Kimber, M.S.,Ching, R.,Sprangers, R.,Fiebig, K.M.,Houry, W.A. The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J.Biol.Chem., 280:16185-16196, 2005 Cited by PubMed: 15701650DOI: 10.1074/jbc.M414124200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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