2KGJ
Solution structure of parvulin domain of PpiD from E.Coli
Summary for 2KGJ
Entry DOI | 10.2210/pdb2kgj/pdb |
NMR Information | BMRB: 16211 |
Descriptor | Peptidyl-prolyl cis-trans isomerase D (1 entity in total) |
Functional Keywords | prolyl isomerase, parvulin, cell inner membrane, cell membrane, isomerase, membrane, rotamase, stress response, transmembrane |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 11173.50 |
Authors | Weininger, U.,Jakob, R.P. (deposition date: 2009-03-12, release date: 2010-01-19, Last modification date: 2020-02-26) |
Primary citation | Weininger, U.,Jakob, R.P.,Kovermann, M.,Balbach, J.,Schmid, F.X. The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity. Protein Sci., 19:6-18, 2009 Cited by PubMed: 19866485DOI: 10.1002/pro.277 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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