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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) |
Authors | Cui, H. / Muller, A.U. / Leibundgut, M. / Tian, J. / Ban, N. / Weber-Ban, E. |
External links | Nat Commun / PubMed:34789727 |
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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Keywords | HYDROLASE / depupylase / Dop-loop / deamidase / Pup / ATP hydrolysis / Pup binding / phosphorylated Pup binding / transition state / product state |