3BGQ
Human Pim-1 kinase in complex with an triazolo pyridazine inhibitor VX2
Summary for 3BGQ
| Entry DOI | 10.2210/pdb3bgq/pdb |
| Related | 3BGP 3BGZ |
| Descriptor | Proto-oncogene serine/threonine-protein kinase Pim-1, N-cyclohexyl-3-[3-(trifluoromethyl)phenyl][1,2,4]triazolo[4,3-b]pyridazin-6-amine (3 entities in total) |
| Functional Keywords | kinase inhibitor phosphorylation, alternative initiation, atp-binding, cytoplasm, manganese, membrane, metal-binding, nucleotide-binding, nucleus, phosphoprotein, proto-oncogene, serine/threonine-protein kinase, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 2: Cytoplasm. Isoform 1: Cell membrane: P11309 |
| Total number of polymer chains | 1 |
| Total formula weight | 38345.44 |
| Authors | Jacobs, M.D. (deposition date: 2007-11-27, release date: 2007-12-11, Last modification date: 2024-10-30) |
| Primary citation | Pierce, A.C.,Jacobs, M.,Stuver-Moody, C. Docking study yields four novel inhibitors of the protooncogene pim-1 kinase. J.Med.Chem., 51:1972-1975, 2008 Cited by PubMed Abstract: To supplement the hits from a high throughput screen, docking was performed against Pim-1 kinase. Glide docking was augmented with a filter to require traditional or aromatic CH..O hydrogen bonds to the kinase hinge. Four diverse actives, of 96 molecules assayed, had K(i) values between 0.091 and 4.5 microM. This gives a 14-fold enrichment over the earlier HTS run, and the two crystal structures solved confirmed the binding modes predicted by docking. PubMed: 18290603DOI: 10.1021/jm701248t PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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