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| Title | Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state. |
|---|---|
| Journal, issue, pages | Acta Crystallogr. ,Sect. D, Vol. 70, Page 833-840, Year 2014 |
| Publish date | Aug 12, 2013 (structure data deposition date) |
Authors | Blankenship, E. / Vukoti, K. / Miyagi, M. / Lodowski, D.T. |
External links | Acta Crystallogr. ,Sect. D / PubMed:24598752 |
| Methods | X-ray diffraction |
| Resolution | 0.81 Å |
| Structure data | ![]() PDB-4m7g: |
| Chemicals | ![]() ChemComp-HOH: |
| Source |
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Keywords | HYDROLASE / Serine Protease |
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saccharopolyspora erythraea (bacteria)
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