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-Structure paper
Title | Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation. |
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Journal, issue, pages | Proc. Natl. Acad. Sci. USA, Vol. 111, Page 17839-17844, Year 2014 |
Publish date | Aug 14, 2014 (structure data deposition date) |
![]() | Rivera-Cancel, G. / Ko, W.H. / Tomchick, D.R. / Correa, F. / Gardner, K.H. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.6 - 2.92 Å |
Structure data | ![]() PDB-4r38: ![]() PDB-4r39: ![]() PDB-4r3a: |
Chemicals | ![]() ChemComp-RBF: ![]() ChemComp-HOH: ![]() ChemComp-MG: ![]() ChemComp-ANP: |
Source |
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![]() | SIGNALING PROTEIN / riboflavin / light-activated / LOV domain / photoreceptor / sensory transduction / signal transduction / TRANSFERASE / histidine kinase domain / Bergerat fold / histidine kinase / cell signaling / regulation / two-component system |