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5V89

Structure of DCN4 PONY domain bound to CUL1 WHB

Summary for 5V89
Entry DOI10.2210/pdb5v89/pdb
Related5V83 5V86 5V88
DescriptorDCN1-like protein 4, Cullin-1 (3 entities in total)
Functional Keywordse3 ligase, ligase - protein binding complex, ligase / protein binding
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight31772.53
Authors
Guy, R.K.,Schulman, B.A.,Scott, D.C.,Hammill, J.T. (deposition date: 2017-03-21, release date: 2017-05-24, Last modification date: 2023-10-04)
Primary citationScott, D.C.,Hammill, J.T.,Min, J.,Rhee, D.Y.,Connelly, M.,Sviderskiy, V.O.,Bhasin, D.,Chen, Y.,Ong, S.S.,Chai, S.C.,Goktug, A.N.,Huang, G.,Monda, J.K.,Low, J.,Kim, H.S.,Paulo, J.A.,Cannon, J.R.,Shelat, A.A.,Chen, T.,Kelsall, I.R.,Alpi, A.F.,Pagala, V.,Wang, X.,Peng, J.,Singh, B.,Harper, J.W.,Schulman, B.A.,Guy, R.K.
Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase.
Nat. Chem. Biol., 13:850-857, 2017
Cited by
PubMed: 28581483
DOI: 10.1038/nchembio.2386
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

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