Summary for 2OLB
| Entry DOI | 10.2210/pdb2olb/pdb |
| Descriptor | OLIGO-PEPTIDE BINDING PROTEIN, TRIPEPTIDE LYS-LYS-LYS, URANYL (VI) ION, ... (5 entities in total) |
| Functional Keywords | periplasmic, complex (binding protein-peptide) complex, complex (binding protein/peptide) |
| Biological source | Salmonella typhimurium |
| Cellular location | Periplasm: P06202 |
| Total number of polymer chains | 2 |
| Total formula weight | 61799.03 |
| Authors | Tame, J.,Wilkinson, A.J. (deposition date: 1995-09-10, release date: 1996-01-29, Last modification date: 2024-10-23) |
| Primary citation | Tame, J.R.,Dodson, E.J.,Murshudov, G.,Higgins, C.F.,Wilkinson, A.J. The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands. Structure, 3:1395-1406, 1995 Cited by PubMed Abstract: The periplasmic oligopeptide-binding protein OppA has a remarkably broad substrate specificity, binding peptides of two or five amino-acid residues with high affinity, but little regard to sequence. It is therefore an ideal system for studying how different chemical groups can be accommodated in a protein interior. The ability of the protein to bind peptides of different lengths has been studied by co-crystallising it with different ligands. PubMed: 8747465DOI: 10.1016/S0969-2126(01)00276-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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