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6YG1

Crystal structure of MKK7 (MAP2K7) in an active state, allosterically triggered by the N-terminal helix

Summary for 6YG1
Entry DOI10.2210/pdb6yg1/pdb
DescriptorDual specificity mitogen-activated protein kinase kinase 7, SODIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordskinase, kinase inhibitor, mkk7, mek7, map2k7, map2k, mek, jnk signaling, structural genomics, structural genomics consortium, sgc, transferase, scottish structural proteomics facility, sspf
Biological sourceHomo sapiens (Human)
Total number of polymer chains3
Total formula weight120409.38
Authors
Chaikuad, A.,Knapp, S.,Structural Genomics Consortium (SGC),Scottish Structural Proteomics Facility (SSPF) (deposition date: 2020-03-27, release date: 2020-08-12, Last modification date: 2024-01-24)
Primary citationSchroder, M.,Tan, L.,Wang, J.,Liang, Y.,Gray, N.S.,Knapp, S.,Chaikuad, A.
Catalytic Domain Plasticity of MKK7 Reveals Structural Mechanisms of Allosteric Activation and Diverse Targeting Opportunities.
Cell Chem Biol, 27:1285-1295.e4, 2020
Cited by
PubMed: 32783966
DOI: 10.1016/j.chembiol.2020.07.014
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.22 Å)
Structure validation

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