5V88
Structure of DCN1 bound to NAcM-COV
Summary for 5V88
Entry DOI | 10.2210/pdb5v88/pdb |
Related | 5V83 5V86 5V89 |
Descriptor | Lysozyme,DCN1-like protein 1, N-{2-[({1-[(2R)-pentan-2-yl]piperidin-4-yl}{[3-(trifluoromethyl)phenyl]carbamoyl}amino)methyl]phenyl}propanamide (3 entities in total) |
Functional Keywords | e3 ligase, hydrolase, ligase - protein binding complex, ligase / protein binding |
Biological source | Enterobacteria phage T4 More |
Total number of polymer chains | 1 |
Total formula weight | 44695.84 |
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 citation | Scott, 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: 28581483DOI: 10.1038/nchembio.2386 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.601 Å) |
Structure validation
Download full validation report