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-Structure paper
Title | Structural basis for activity regulation of MLL family methyltransferases. |
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Journal, issue, pages | Nature, Vol. 530, Page 447-452, Year 2016 |
Publish date | Dec 4, 2015 (structure data deposition date) |
![]() | Li, Y. / Han, J. / Zhang, Y. / Cao, F. / Liu, Z. / Li, S. / Wu, J. / Hu, C. / Wang, Y. / Shuai, J. ...Li, Y. / Han, J. / Zhang, Y. / Cao, F. / Liu, Z. / Li, S. / Wu, J. / Hu, C. / Wang, Y. / Shuai, J. / Chen, J. / Cao, L. / Li, D. / Shi, P. / Tian, C. / Zhang, J. / Dou, Y. / Li, G. / Chen, Y. / Lei, M. |
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Methods | X-ray diffraction |
Resolution | 1.802 - 2.801 Å |
Structure data | ![]() PDB-5f59: ![]() PDB-5f5e: ![]() PDB-5f6k: ![]() PDB-5f6l: |
Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-SAH: ![]() ChemComp-HOH: |
Source |
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![]() | TRANSFERASE / Histone methylation / histone methyltransferase / SET domain / TRANSFERASE/PROTEIN BINDING / MLL-family proteins / TRANSFERASE-PROTEIN BINDING complex / PROTEIN BINDING/TRANSFERASE / protein complex / PROTEIN BINDING-TRANSFERASE complex |