5KHX
Crystal structure of JAK1 in complex with PF-4950736
Summary for 5KHX
| Entry DOI | 10.2210/pdb5khx/pdb |
| Descriptor | Tyrosine-protein kinase JAK1, ~{N}-[3-[methyl(7~{H}-pyrrolo[2,3-d]pyrimidin-4-yl)amino]cyclobutyl]methanesulfonamide (3 entities in total) |
| Functional Keywords | jak1, kinase, inhibitor, complex, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Homo sapiens (Human) |
| Cellular location | Endomembrane system; Peripheral membrane protein: P23458 |
| Total number of polymer chains | 1 |
| Total formula weight | 36712.83 |
| Authors | Han, S.,Caspers, N.L. (deposition date: 2016-06-16, release date: 2016-11-09, Last modification date: 2024-10-16) |
| Primary citation | Caspers, N.L.,Han, S.,Rajamohan, F.,Hoth, L.R.,Geoghegan, K.F.,Subashi, T.A.,Vazquez, M.L.,Kaila, N.,Cronin, C.N.,Johnson, E.,Kurumbail, R.G. Development of a high-throughput crystal structure-determination platform for JAK1 using a novel metal-chelator soaking system. Acta Crystallogr F Struct Biol Commun, 72:840-845, 2016 Cited by PubMed Abstract: Crystals of phosphorylated JAK1 kinase domain were initially generated in complex with nucleotide (ADP) and magnesium. The tightly bound Mg-ADP at the ATP-binding site proved recalcitrant to ligand displacement. Addition of a molar excess of EDTA helped to dislodge the divalent metal ion, promoting the release of ADP and allowing facile exchange with ATP-competitive small-molecule ligands. Many kinases require the presence of a stabilizing ligand in the ATP site for crystallization. This procedure could be useful for developing co-crystallization systems with an exchangeable ligand to enable structure-based drug design of other protein kinases. PubMed: 27827355DOI: 10.1107/S2053230X16016356 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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