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4LMN

Crystal Structure of MEK1 kinase bound to GDC0973

Summary for 4LMN
Entry DOI10.2210/pdb4lmn/pdb
Related3V01
DescriptorDual specificity mitogen-activated protein kinase kinase 1, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordskinase, phosphorylation, braf, transferase-transferase inhibitor complex, transferase/transferase inhibitor
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm, cytoskeleton, microtubule organizing center, centrosome: Q02750
Total number of polymer chains1
Total formula weight38992.42
Authors
Ultsch, M.H. (deposition date: 2013-07-10, release date: 2013-08-07, Last modification date: 2024-02-28)
Primary citationHatzivassiliou, G.,Haling, J.R.,Chen, H.,Song, K.,Price, S.,Heald, R.,Hewitt, J.F.,Zak, M.,Peck, A.,Orr, C.,Merchant, M.,Hoeflich, K.P.,Chan, J.,Luoh, S.M.,Anderson, D.J.,Ludlam, M.J.,Wiesmann, C.,Ultsch, M.,Friedman, L.S.,Malek, S.,Belvin, M.
Mechanism of MEK inhibition determines efficacy in mutant KRAS- versus BRAF-driven cancers.
Nature, 501:232-236, 2013
Cited by
PubMed: 23934108
DOI: 10.1038/nature12441
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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