2oi4 | pdb_00002oi4

Crystal structure of human PIM1 in complex with fluorinated ruthenium pyridocarbazole

spinqualitylabelsall models 2oi4, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2oi4 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, EDO, EPE, JM1 Related: 2bzh, 2bzi, 2bzj, 1yhs Gene: PIM1 (Homo sapiens) Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed A general route to ruthenium pyridocarbazole half-sandwich complexes is presented and applied to the synthesis of sixteen new compounds, many of which have modulated protein kinase inhibition properties. For example, the incorporation of a fluorine into the pyridine moiety increases the binding affinity for glycogen synthase kinase 3 by almost one order of magnitude. These data are supplemented with cyclic voltammetry experiments and a protein co-crystallographic study. Ruthenium half-sandwich complexes as protein kinase inhibitors: derivatization of the pyridocarbazole pharmacophore ligand.,Pagano N, Maksimoska J, Bregman H, Williams DS, Webster RD, Xue F, Meggers E Org Biomol Chem. 2007 Apr 21;5(8):1218-27. Epub 2007 Mar 20. PMID:17406720 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Proto-oncogene serine/threonine-protein kinase

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