1JVP
Crystal structure of human CDK2 (unphosphorylated) in complex with PKF049-365
Summary for 1JVP
| Entry DOI | 10.2210/pdb1jvp/pdb |
| Descriptor | Cell division protein kinase 2, 3-pyridin-4-yl-2,4-dihydroindeno[1,2-c]pyrazole (3 entities in total) |
| Functional Keywords | protein kinase, cell division, cell cycle, enzyme inhibitors, drug design, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 34209.76 |
| Authors | Rondeau, J.M. (deposition date: 2001-08-31, release date: 2001-12-21, Last modification date: 2024-02-07) |
| Primary citation | Furet, P.,Meyer, T.,Strauss, A.,Raccuglia, S.,Rondeau, J.M. Structure-based design and protein X-ray analysis of a protein kinase inhibitor. Bioorg.Med.Chem.Lett., 12:221-224, 2002 Cited by PubMed Abstract: A 5-aryl-1H-pyrazole molecular scaffold was designed to ligate the ATP binding site of cyclin dependent kinase 2 (CDK2) on the basis of crystallographic information. A search of the compound collection of Novartis using this scaffold as substructure query led to the identification of PKF049-365 as a representative of a new class of inhibitors of the cell cycle kinases CDK1/2. The three-dimensional structure of CDK2 in complex with PKF049-365 was subsequently determined by protein crystallography and refined to 1.53 A resolution. The X-ray analysis confirmed the binding mode expected from the design hypothesis. In addition, it revealed an alternative binding orientation involving a second tautomeric form of the inhibitor that was not envisaged during the design stage. PubMed: 11755359DOI: 10.1016/S0960-894X(01)00715-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.53 Å) |
Structure validation
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