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3QYZ

Crystal structure of ERK2 in complex with an inhibitor

Summary for 3QYZ
Entry DOI10.2210/pdb3qyz/pdb
Related3QYU 3QYW
DescriptorMitogen-activated protein kinase 1, 5'-azido-8-bromo-5'-deoxyadenosine, DIMETHYL SULFOXIDE, ... (6 entities in total)
Functional Keywordstransferase, serine/threonine-protein kinase, atp-binding cell cycle, phosphorylation, protein kinase, transferase-transferase inhibitor complex, transferase/transferase inhibitor
Biological sourceRattus norvegicus (brown rat,rat,rats)
Cellular locationCytoplasm, cytoskeleton, spindle : P63086
Total number of polymer chains1
Total formula weight43736.42
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: 2017-11-08)
Primary citationle 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: 21904027
DOI: 10.1107/S0907444911023249
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.46 Å)
Structure validation

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