3S04
Crystal structure of Escherichia coli type I signal peptidase in complex with an Arylomycin Lipoglycopeptide Antibiotic
Summary for 3S04
Entry DOI | 10.2210/pdb3s04/pdb |
Related | 1B12 1KN9 1T7D 3IIQ |
Related PRD ID | PRD_000813 |
Descriptor | Signal peptidase I, Glyco-Arylomycin, 14-methylhexadec-9-enoic acid, ... (5 entities in total) |
Functional Keywords | mostly-beta fold, membrane bound, serine protease, secreted preproteins, cytoplasmic membrane, hydrolase-antibiotic complex, signal peptidase, leader peptidase, signal peptide, leader peptide, serine-lysine dyad, hydrolase/antibiotic |
Biological source | Escherichia coli More |
Cellular location | Cell inner membrane; Multi-pass membrane protein: P00803 |
Total number of polymer chains | 4 |
Total formula weight | 58346.16 |
Authors | Paetzel, M.,Luo, C. (deposition date: 2011-05-13, release date: 2011-10-05, Last modification date: 2023-12-06) |
Primary citation | Liu, J.,Luo, C.,Smith, P.A.,Chin, J.K.,Page, M.G.,Paetzel, M.,Romesberg, F.E. Synthesis and characterization of the arylomycin lipoglycopeptide antibiotics and the crystallographic analysis of their complex with signal peptidase. J.Am.Chem.Soc., 133:17869-17877, 2011 Cited by PubMed: 21999324DOI: 10.1021/ja207318n PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.44 Å) |
Structure validation
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