2OI4

Crystal structure of human PIM1 in complex with fluorinated ruthenium pyridocarbazole

Summary for 2OI4

Entry DOI	10.2210/pdb2oi4/pdb
Related	1YHS 2BZH 2BZI 2BZJ
Descriptor	Proto-oncogene serine/threonine-protein kinase Pim-1, CHLORIDE ION, FLUORINATED PYRIDOCARBAZOLE CYCLOPENTADIENYL RU(CO) COMPLEX, ... (6 entities in total)
Functional Keywords	transferase, pim1, kinase, atp-binding, phosphorylation
Biological source	Homo sapiens (human)
Cellular location	Isoform 2: Cytoplasm. Isoform 1: Cell membrane: P11309
Total number of polymer chains	1
Total formula weight	36590.99
Authors	Maksimoska, J.,Meggers, E. (deposition date: 2007-01-10, release date: 2007-04-10, Last modification date: 2023-12-27)
Primary citation	Pagano, N.,Maksimoska, J.,Bregman, H.,Williams, D.S.,Webster, R.D.,Xue, F.,Meggers, E. Ruthenium half-sandwich complexes as protein kinase inhibitors: derivatization of the pyridocarbazole pharmacophore ligand. Org.Biomol.Chem., 5:1218-1227, 2007 Cited by PubMed Abstract: 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. PubMed: 17406720 DOI: 10.1039/b700433h PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation