3TCH
Crystal structure of E. coli OppA in an open conformation
Summary for 3TCH
Entry DOI | 10.2210/pdb3tch/pdb |
Related | 3TCF 3TCG |
Descriptor | Periplasmic oligopeptide-binding protein (2 entities in total) |
Functional Keywords | peptide-binding domain, protein transport, peptide transport, abc transporter |
Biological source | Escherichia coli |
Cellular location | Periplasm: P23843 |
Total number of polymer chains | 1 |
Total formula weight | 59387.63 |
Authors | Klepsch, M.M.,Kovermann, M.,Low, C.,Balbach, J.,de Gier, J.W.,Slotboom, D.J.,Berntsson, R.P.-A. (deposition date: 2011-08-09, release date: 2011-10-12, Last modification date: 2012-01-11) |
Primary citation | Klepsch, M.M.,Kovermann, M.,Low, C.,Balbach, J.,Permentier, H.P.,Fusetti, F.,de Gier, J.W.,Slotboom, D.J.,Berntsson, R.P. Escherichia coli peptide binding protein OppA has a preference for positively charged peptides. J.Mol.Biol., 414:75-85, 2011 Cited by PubMed: 21983341DOI: 10.1016/j.jmb.2011.09.043 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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