5XXK
Structure-activity studies of Mdm2/Mdm4-binding stapled peptides comprising non-natural amino acids
Summary for 5XXK
Entry DOI | 10.2210/pdb5xxk/pdb |
Descriptor | E3 ubiquitin-protein ligase Mdm2, Hydrocarbon stapled peptide THC-SER-PHE-0EH-GLU-TYR-6CW-ALA-LEU-LEU-MK8-NH2 (3 entities in total) |
Functional Keywords | e3 ubiqutin ligase, oncoprotein, oncoprotein-inhibitor complex, oncoprotein/inhibitor |
Biological source | Homo sapiens (Human) More |
Cellular location | Nucleus, nucleoplasm: Q00987 |
Total number of polymer chains | 4 |
Total formula weight | 30379.55 |
Authors | Brown, C.J. (deposition date: 2017-07-04, release date: 2017-12-27, Last modification date: 2023-11-22) |
Primary citation | Chee, S.M.Q.,Wongsantichon, J.,Siau, J.,Thean, D.,Ferrer, F.,Robinson, R.C.,Lane, D.P.,Brown, C.J.,Ghadessy, F.J. Structure-activity studies of Mdm2/Mdm4-binding stapled peptides comprising non-natural amino acids. PLoS ONE, 12:e0189379-e0189379, 2017 Cited by PubMed: 29228061DOI: 10.1371/journal.pone.0189379 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.66 Å) |
Structure validation
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