3NWW
P38 Alpha kinase complexed with a 2-aminothiazol-5-yl-pyrimidine based inhibitor
Summary for 3NWW
| Entry DOI | 10.2210/pdb3nww/pdb |
| Descriptor | Mitogen-activated protein kinase 14, 1-[2-(2-{[2-(dimethylamino)ethyl]amino}-6-{2-[(1-methylethyl)amino]-1,3-thiazol-5-yl}pyrimidin-4-yl)benzyl]-3-ethylurea (3 entities in total) |
| Functional Keywords | p38 map kinase, serine/threonine-protein kinase, transferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 42587.65 |
| Authors | Sack, J.S. (deposition date: 2010-07-12, release date: 2010-09-08, Last modification date: 2024-02-21) |
| Primary citation | Lin, S.,Wrobleski, S.T.,Hynes, J.,Pitt, S.,Zhang, R.,Fan, Y.,Doweyko, A.M.,Kish, K.F.,Sack, J.S.,Malley, M.F.,Kiefer, S.E.,Newitt, J.A.,McKinnon, M.,Trzaskos, J.,Barrish, J.C.,Dodd, J.H.,Schieven, G.L.,Leftheris, K. Utilization of a nitrogen-sulfur nonbonding interaction in the design of new 2-aminothiazol-5-yl-pyrimidines as p38alpha MAP kinase inhibitors. Bioorg.Med.Chem.Lett., 20:5864-5868, 2010 Cited by PubMed Abstract: The design, synthesis, and structure-activity relationships (SAR) of a series of 2-aminothiazol-5-yl-pyrimidines as novel p38α MAP kinase inhibitors are described. These efforts led to the identification of 41 as a potent p38α inhibitor that utilizes a unique nitrogen-sulfur intramolecular nonbonding interaction to stabilize the conformation required for binding to the p38α active site. X-ray crystallographic studies that confirm the proposed binding mode of this class of inhibitors in p38 α and provide evidence for the proposed intramolecular nitrogen-sulfur interaction are discussed. PubMed: 20732813DOI: 10.1016/j.bmcl.2010.07.102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
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