1B12
CRYSTAL STRUCTURE OF TYPE 1 SIGNAL PEPTIDASE FROM ESCHERICHIA COLI IN COMPLEX WITH A BETA-LACTAM INHIBITOR
Summary for 1B12
Entry DOI | 10.2210/pdb1b12/pdb |
Descriptor | SIGNAL PEPTIDASE I, prop-2-en-1-yl (2S)-2-[(2S,3R)-3-(acetyloxy)-1-oxobutan-2-yl]-2,3-dihydro-1,3-thiazole-4-carboxylate, PHOSPHATE ION, ... (4 entities in total) |
Functional Keywords | serine proteinase, serine-dependant hydrolase, signal peptide processing, protein translocation, membrane bound proteinase, membrane protein, hydrolase |
Biological source | Escherichia coli |
Cellular location | Cell inner membrane; Multi-pass membrane protein: P00803 |
Total number of polymer chains | 4 |
Total formula weight | 112634.20 |
Authors | Paetzel, M.,Dalbey, R.,Strynadka, N.C.J. (deposition date: 1999-11-24, release date: 1999-12-10, Last modification date: 2023-12-27) |
Primary citation | Paetzel, M.,Dalbey, R.E.,Strynadka, N.C. Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature, 396:186-190, 1998 Cited by PubMed: 9823901DOI: 10.1038/24196 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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