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| Title | Achieving thermostability of a phytase with resistance up to 100 °C. |
|---|---|
| Journal, issue, pages | J. Biol. Chem., Vol. 300, Page 107992-107992, Year 2024 |
| Publish date | Dec 27, 2023 (structure data deposition date) |
Authors | Tu, T. / Wang, Q. / Dong, R. / Liu, X. / Penttinen, L. / Hakulinen, N. / Tian, J. / Zhang, W. / Wang, Y. / Luo, H. ...Tu, T. / Wang, Q. / Dong, R. / Liu, X. / Penttinen, L. / Hakulinen, N. / Tian, J. / Zhang, W. / Wang, Y. / Luo, H. / Yao, B. / Huang, H. |
External links | J. Biol. Chem. / PubMed:39547510 |
| Methods | X-ray diffraction |
| Resolution | 1.77 - 1.9 Å |
| Structure data | ![]() PDB-8xm1: ![]() PDB-8xm2: |
| Chemicals | ![]() ChemComp-TRS: ![]() ChemComp-HOH: |
| Source |
|
Keywords | HYDROLASE / Phytase mutant APPAmut4 / The mutant crystal structure of phytase APPAmut9 from Yersinia intermedia |
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yersinia intermedia (bacteria)
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