1KN9
CRYSTAL STRUCTURE OF A BACTERIAL SIGNAL PEPTIDASE APO-ENZYME, IMPLICATIONS FOR SIGNAL PEPTIDE BINDING AND THE SER-LYS DYAD MECHANISM.
Summary for 1KN9
Entry DOI | 10.2210/pdb1kn9/pdb |
Related | 1B12 |
Descriptor | Signal peptidase I (2 entities in total) |
Functional Keywords | serine protease, lysine general base, membrane protein, mostly beta-fold, hydrolase |
Biological source | Escherichia coli K12 |
Cellular location | Cell inner membrane ; Multi-pass membrane protein : P00803 |
Total number of polymer chains | 4 |
Total formula weight | 111866.63 |
Authors | Paetzel, M.,Dalbey, R.E.,Strynadka, N.C.J. (deposition date: 2001-12-18, release date: 2002-01-30, Last modification date: 2023-08-16) |
Primary citation | Paetzel, M.,Dalbey, R.E.,Strynadka, N.C.J. Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism J.Biol.Chem., 277:9512-9519, 2002 Cited by PubMed: 11741964DOI: 10.1074/jbc.M110983200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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