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-Structure paper
Title | Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation. |
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Journal, issue, pages | Nat Commun, Vol. 12, Page 6635-6635, Year 2021 |
Publish date | Jun 23, 2021 (structure data deposition date) |
![]() | Cui, H. / Muller, A.U. / Leibundgut, M. / Tian, J. / Ban, N. / Weber-Ban, E. |
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Methods | X-ray diffraction |
Resolution | 1.394 - 1.88 Å |
Structure data | ![]() PDB-7oxv: ![]() PDB-7oxy: ![]() PDB-7oy3: ![]() PDB-7oyf: ![]() PDB-7oyh: |
Chemicals | ![]() ChemComp-PGE: ![]() ChemComp-SCN: ![]() ChemComp-PEG: ![]() ChemComp-EDO: ![]() ChemComp-HOH: ![]() ChemComp-MG: ![]() ChemComp-ACP: ![]() ChemComp-ACT: ![]() ChemComp-K: ![]() ChemComp-ADP: ![]() ChemComp-KQB: ![]() ChemComp-SO4: ![]() ChemComp-MF4: |
Source |
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![]() | HYDROLASE / depupylase / Dop-loop / deamidase / Pup / ATP hydrolysis / Pup binding / phosphorylated Pup binding / transition state / product state |