3QYW
Crystal structure of ERK2 in complex with an inhibitor
Summary for 3QYW
| Entry DOI | 10.2210/pdb3qyw/pdb |
| Related | 3QYU 3QYZ |
| Descriptor | Mitogen-activated protein kinase 1, 6-(3-bromophenyl)-7H-purin-2-amine, DIMETHYL SULFOXIDE, ... (5 entities in total) |
| Functional Keywords | transferase, serine/threonine-protein kinase, atp-binding cell cycle, phosphorylation, protein kinase, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Rattus norvegicus (brown rat,rat,rats) |
| Cellular location | Cytoplasm, cytoskeleton, spindle : P63086 |
| Total number of polymer chains | 1 |
| Total formula weight | 43403.06 |
| Authors | Gelin, M.,Pochet, S.,Hoh, F.,Pirochi, M.,Guichou, J.-F.,Ferrer, J.-L.,Labesse, G. (deposition date: 2011-03-04, release date: 2011-08-24, Last modification date: 2024-10-30) |
| Primary citation | le Maire, A.,Gelin, M.,Pochet, S.,Hoh, F.,Pirocchi, M.,Guichou, J.F.,Ferrer, J.L.,Labesse, G. In-plate protein crystallization, in situ ligand soaking and X-ray diffraction. Acta Crystallogr.,Sect.D, 67:747-755, 2011 Cited by PubMed Abstract: X-ray crystallography is now a recognized technique for ligand screening, especially for fragment-based drug design. However, protein crystal handling is still tedious and limits further automation. An alternative method for the solution of crystal structures of proteins in complex with small ligands is proposed. Crystallization drops are directly exposed to an X-ray beam after cocrystallization or soaking with the desired ligands. The use of dedicated plates in connection with an optimal parametrization of the G-rob robot allows efficient data collection. Three proteins currently under study in our laboratory for ligand screening by X-ray crystallography were used as validation test cases. The protein crystals belonged to different space groups, including a challenging monoclinic case. The resulting diffraction data can lead to clear ligand recognition, including indication of alternating conformations. These results demonstrate a possible method for automation of ligand screening by X-ray crystallography. PubMed: 21904027DOI: 10.1107/S0907444911023249 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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