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4XOZ

Crystal structure of ERK2 in complex with an inhibitor

Summary for 4XOZ
Entry DOI10.2210/pdb4xoz/pdb
DescriptorMitogen-activated protein kinase 1, N~1~-[3-(benzyloxy)benzyl]-1H-tetrazole-1,5-diamine, SULFATE ION, ... (4 entities in total)
Functional Keywordsserine/threonine-protein kinase, transferase
Biological sourceRattus norvegicus (norway Rat)
Cellular locationCytoplasm, cytoskeleton, spindle : P63086
Total number of polymer chains1
Total formula weight41241.40
Authors
Gelin, M.,Allemand, F.,Labesse, G.,Guichou, J.F. (deposition date: 2015-01-16, release date: 2015-08-12, Last modification date: 2024-11-20)
Primary citationGelin, M.,Delfosse, V.,Allemand, F.,Hoh, F.,Sallaz-Damaz, Y.,Pirocchi, M.,Bourguet, W.,Ferrer, J.L.,Labesse, G.,Guichou, J.F.
Combining `dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-ray crystallography.
Acta Crystallogr.,Sect.D, 71:1777-1787, 2015
Cited by
PubMed Abstract: X-ray crystallography is an established technique for ligand screening in fragment-based drug-design projects, but the required manual handling steps - soaking crystals with ligand and the subsequent harvesting - are tedious and limit the throughput of the process. Here, an alternative approach is reported: crystallization plates are pre-coated with potential binders prior to protein crystallization and X-ray diffraction is performed directly 'in situ' (or in-plate). Its performance is demonstrated on distinct and relevant therapeutic targets currently being studied for ligand screening by X-ray crystallography using either a bending-magnet beamline or a rotating-anode generator. The possibility of using DMSO stock solutions of the ligands to be coated opens up a route to screening most chemical libraries.
PubMed: 26249358
DOI: 10.1107/S1399004715010342
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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