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-Structure paper
Title | Allomorphy as a mechanism of post-translational control of enzyme activity. |
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Journal, issue, pages | Nat Commun, Vol. 11, Page 5538-5538, Year 2020 |
Publish date | Mar 20, 2020 (structure data deposition date) |
![]() | Wood, H.P. / Cruz-Navarrete, F.A. / Baxter, N.J. / Trevitt, C.R. / Robertson, A.J. / Dix, S.R. / Hounslow, A.M. / Cliff, M.J. / Waltho, J.P. |
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Methods | X-ray diffraction |
Resolution | 1.04 - 2.1 Å |
Structure data | ![]() PDB-6ydj: ![]() PDB-6ydk: ![]() PDB-6ydl: ![]() PDB-6ydm: |
Chemicals | ![]() ChemComp-BG6: ![]() ChemComp-MGF: ![]() ChemComp-MG: ![]() ChemComp-NA: ![]() ChemComp-EDO: ![]() ChemComp-PDO: ![]() ChemComp-HOH: ![]() ChemComp-CIT: ![]() ChemComp-ACT: ![]() ChemComp-TRS: |
Source |
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![]() | ISOMERASE / transition-state analogue / cis-trans proline isomerization / allomorphy / phosphoryl transfer / enzyme regulation / citrate |