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5XXK

Structure-activity studies of Mdm2/Mdm4-binding stapled peptides comprising non-natural amino acids

Summary for 5XXK
Entry DOI10.2210/pdb5xxk/pdb
DescriptorE3 ubiquitin-protein ligase Mdm2, Hydrocarbon stapled peptide THC-SER-PHE-0EH-GLU-TYR-6CW-ALA-LEU-LEU-MK8-NH2 (3 entities in total)
Functional Keywordse3 ubiqutin ligase, oncoprotein, oncoprotein-inhibitor complex, oncoprotein/inhibitor
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus, nucleoplasm: Q00987
Total number of polymer chains4
Total formula weight30379.55
Authors
Brown, C.J. (deposition date: 2017-07-04, release date: 2017-12-27, Last modification date: 2023-11-22)
Primary citationChee, 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: 29228061
DOI: 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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