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; PubMed: 31279627; DOI: 10.1016/j.str.2019.06.005

Experimental method

X-RAY DIFFRACTION (1.086 Å)