7LZB
Crystal Structure of SETD2 bound to Compound 2
Summary for 7LZB
| Entry DOI | 10.2210/pdb7lzb/pdb |
| Descriptor | Histone-lysine N-methyltransferase SETD2, ZINC ION, S-ADENOSYLMETHIONINE, ... (6 entities in total) |
| Functional Keywords | transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 32970.72 |
| Authors | Farrow, N.A.,Boriack-Sjodin, P. (deposition date: 2021-03-09, release date: 2021-09-22, Last modification date: 2023-10-18) |
| Primary citation | Lampe, J.W.,Alford, J.S.,Boriak-Sjodin, P.A.,Brach, D.,Cosmopoulos, K.,Duncan, K.W.,Eckley, S.T.,Foley, M.A.,Harvey, D.M.,Motwani, V.,Munchhof, M.J.,Raimondi, A.,Riera, T.V.,Tang, C.,Thomenius, M.J.,Totman, J.,Farrow, N.A. Discovery of a First-in-Class Inhibitor of the Histone Methyltransferase SETD2 Suitable for Preclinical Studies. Acs Med.Chem.Lett., 12:1539-1545, 2021 Cited by PubMed Abstract: SET domain-containing protein 2 (SETD2), a histone methyltransferase, has been identified as a target of interest in certain hematological malignancies, including multiple myeloma. This account details the discovery of , a novel and potent SETD2 inhibitor with a high selectivity over other histone methyltransferases. A screening campaign of the Epizyme proprietary histone methyltransferase-biased library identified potential leads based on a 2-amidoindole core. Structure-based drug design (SBDD) and drug metabolism/pharmacokinetics (DMPK) optimization resulted in , an attractive tool compound for the interrogation of SETD2 biology that enables target validation studies. PubMed: 34671445DOI: 10.1021/acsmedchemlett.1c00272 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.28 Å) |
Structure validation
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