6GY5
Crystal structure of the kelch domain of human KLHL20 in complex with DAPK1 peptide
Summary for 6GY5
Entry DOI | 10.2210/pdb6gy5/pdb |
Descriptor | Kelch-like protein 20, Death-associated protein kinase 1, CHLORIDE ION, ... (6 entities in total) |
Functional Keywords | complex, e3 ligase, substrate, ubiquitination, kelch domain, death domain, ligase |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 2 |
Total formula weight | 35274.69 |
Authors | Chen, Z.,Hozjan, V.,Strain-Damerell, C.,Williams, E.,Wang, D.,Cooper, C.D.O.,Sanvitale, C.E.,Fairhead, M.,Carpenter, E.P.,Pike, A.C.W.,Krojer, T.,Srikannathasan, V.,Sorrell, F.,Johansson, C.,Mathea, S.,Burgess-Brown, N.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.M.,Bountra, C.,Bullock, A.N. (deposition date: 2018-06-28, release date: 2018-08-08, Last modification date: 2024-01-17) |
Primary citation | Chen, Z.,Picaud, S.,Filippakopoulos, P.,D'Angiolella, V.,Bullock, A.N. Structural Basis for Recruitment of DAPK1 to the KLHL20 E3 Ligase. Structure, 27:1395-1404.e4, 2019 Cited by PubMed: 31279627DOI: 10.1016/j.str.2019.06.005 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.086 Å) |
Structure validation
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