2PV3
Crystallographic Structure of SurA fragment lacking the second peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK
Summary for 2PV3
Entry DOI | 10.2210/pdb2pv3/pdb |
Descriptor | Chaperone surA, C-peptide (2 entities in total) |
Functional Keywords | survival protein a, peptidyl-prolyl cis-trans isomerase domain, isomerase |
Biological source | Escherichia coli More |
Cellular location | Periplasm: P0ABZ6 P0ABZ6 |
Total number of polymer chains | 3 |
Total formula weight | 68061.15 |
Authors | Xu, X.,McKay, D.B. (deposition date: 2007-05-09, release date: 2007-10-02, Last modification date: 2023-08-30) |
Primary citation | Xu, X.,Wang, S.,Hu, Y.X.,McKay, D.B. The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues. J.Mol.Biol., 373:367-381, 2007 Cited by PubMed: 17825319DOI: 10.1016/j.jmb.2007.07.069 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.39 Å) |
Structure validation
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