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-Structure paper
Title | Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain. |
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Journal, issue, pages | Febs J., Vol. 287, Page 2235-2255, Year 2020 |
Publish date | Feb 24, 2017 (structure data deposition date) |
![]() | Shabalin, I.G. / Gritsunov, A. / Hou, J. / Slawek, J. / Miks, C.D. / Cooper, D.R. / Minor, W. / Christendat, D. |
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Methods | X-ray diffraction |
Resolution | 2.01 - 2.75 Å |
Structure data | ![]() PDB-5uyy: ![]() PDB-5v0s: ![]() PDB-6cxd: ![]() PDB-6u60: |
Chemicals | ![]() ChemComp-TYR: ![]() ChemComp-HOH: ![]() ChemComp-SO4: ![]() ChemComp-CA: ![]() ChemComp-PO4: ![]() ChemComp-NAD: |
Source |
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![]() | OXIDOREDUCTASE / prephenate dehydrogenase / tyrA / Bacillus anthracis / CSGID / Structural Genomics / Center for Structural Genomics of Infectious Diseases / HYDROLASE / peptidase B |