1TYF
THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS
Summary for 1TYF
Entry DOI | 10.2210/pdb1tyf/pdb |
Descriptor | CLP PEPTIDASE (2 entities in total) |
Functional Keywords | peptidase |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P0A6G7 |
Total number of polymer chains | 14 |
Total formula weight | 302216.08 |
Authors | Wang, J.,Hartling, J.A.,Flanagan, J.M. (deposition date: 1997-10-13, release date: 1998-06-17, Last modification date: 2024-02-14) |
Primary citation | Wang, J.,Hartling, J.A.,Flanagan, J.M. The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis. Cell(Cambridge,Mass.), 91:447-456, 1997 Cited by PubMed: 9390554DOI: 10.1016/S0092-8674(00)80431-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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