6YG1
Crystal structure of MKK7 (MAP2K7) in an active state, allosterically triggered by the N-terminal helix
Summary for 6YG1
Entry DOI | 10.2210/pdb6yg1/pdb |
Descriptor | Dual specificity mitogen-activated protein kinase kinase 7, SODIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | kinase, kinase inhibitor, mkk7, mek7, map2k7, map2k, mek, jnk signaling, structural genomics, structural genomics consortium, sgc, transferase, scottish structural proteomics facility, sspf |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 3 |
Total formula weight | 120409.38 |
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 citation | Schroder, 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: 32783966DOI: 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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