6KZU

Macrocyclization of an all-D linear peptide improves target affinity and imparts cellular activity: A novel stapled alpha-helical peptide modality

Summary for 6KZU

Entry DOI	10.2210/pdb6kzu/pdb
Descriptor	E3 ubiquitin-protein ligase Mdm2, 2JN-DAL-E03-DTY-2JN-DSG-TDF-DGL-MK8-DLE-DLE-2JN (3 entities in total)
Functional Keywords	e3 ligase, ligase
Biological source	Homo sapiens (Human) More
Total number of polymer chains	2
Total formula weight	15399.60
Authors	Jiang, S.,Brown, C.J. (deposition date: 2019-09-25, release date: 2019-10-16, Last modification date: 2023-11-22)
Primary citation	Kannan, S.,Aronica, P.G.A.,Ng, S.,Gek Lian, D.T.,Frosi, Y.,Chee, S.,Shimin, J.,Yuen, T.Y.,Sadruddin, A.,Kaan, H.Y.K.,Chandramohan, A.,Wong, J.H.,Tan, Y.S.,Chang, Z.W.,Ferrer-Gago, F.J.,Arumugam, P.,Han, Y.,Chen, S.,Renia, L.,Brown, C.J.,Johannes, C.W.,Henry, B.,Lane, D.P.,Sawyer, T.K.,Verma, C.S.,Partridge, A.W. Macrocyclization of an all-d linear alpha-helical peptide imparts cellular permeability. Chem Sci, 11:5577-5591, 2020 Cited by PubMed: 32874502 DOI: 10.1039/c9sc06383h PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.79 Å)

Structure validation