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-Structure paper
Title | Structural and Biophysical Analysis of the Phytochelatin-Synthase-Like Enzyme from Nostoc sp. Shows That Its Protease Activity is Sensitive to the Redox State of the Substrate. |
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Journal, issue, pages | Acs Chem. Biol., Vol. 17, Page 883-897, Year 2022 |
Publish date | Nov 20, 2019 (structure data deposition date) |
Authors | Gisdon, F.J. / Feiler, C.G. / Kempf, O. / Foerster, J.M. / Haiss, J. / Blankenfeldt, W. / Ullmann, G.M. / Bombarda, E. |
External links | Acs Chem. Biol. / PubMed:35377603 |
Methods | X-ray diffraction |
Resolution | 1.09 Å |
Structure data | PDB-6tho: |
Chemicals | ChemComp-GDS: ChemComp-CA: ChemComp-HOH: |
Source |
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Keywords | TRANSFERASE / glutathione / phytochelatin / detoxification / chelating heavy atoms |