3FY0
Crystal structure of PAK1 kinase domain with ruthenium complex DW1
Summary for 3FY0
| Entry DOI | 10.2210/pdb3fy0/pdb |
| Related | 3FXZ |
| Descriptor | Serine/threonine-protein kinase PAK 1, Ruthenium pyridocarbazole (3 entities in total) |
| Functional Keywords | transferase, kinase, atp-binding, phosphorylation, allosteric enzyme, apoptosis, cell junction, nucleotide-binding, phosphoprotein, serine/threonine-protein kinase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : Q13153 |
| Total number of polymer chains | 1 |
| Total formula weight | 33863.68 |
| Authors | Maksimoska, J.,Marmorstein, R.,Meggers, E. (deposition date: 2009-01-21, release date: 2009-03-03, Last modification date: 2024-11-06) |
| Primary citation | Maksimoska, J.,Feng, L.,Harms, K.,Yi, C.,Kissil, J.,Marmorstein, R.,Meggers, E. Targeting Large Kinase Active Site with Rigid, Bulky Octahedral Ruthenium Complexes J.Am.Chem.Soc., 130:15764-15765, 2008 Cited by PubMed Abstract: A strategy for targeting protein kinases with large ATP-binding sites by using bulky and rigid octahedral ruthenium complexes as structural scaffolds is presented. A highly potent and selective GSK3 and Pim1 half-sandwich complex NP309 was successfully converted into a PAK1 inhibitor by making use of the large octahedral compounds Lambda-FL172 and Lambda-FL411 in which the cyclopentadienyl moiety of NP309 is replaced by a chloride and sterically demanding diimine ligands. A 1.65 A cocrystal structure of PAK1 with Lambda-FL172 reveals how the large coordination sphere of the ruthenium complex matches the size of the active site and serves as a yardstick to discriminate between otherwise closely related binding sites. PubMed: 18973295PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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