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-Structure paper
| Title | Residues W215, E217 and E192 control the allosteric E*-E equilibrium of thrombin. |
|---|---|
| Journal, issue, pages | Sci Rep, Vol. 9, Page 12304-12304, Year 2019 |
| Publish date | Jun 10, 2019 (structure data deposition date) |
Authors | Pelc, L.A. / Koester, S.K. / Chen, Z. / Gistover, N.E. / Di Cera, E. |
External links | Sci Rep / PubMed:31444378 |
| Methods | X-ray diffraction |
| Resolution | 2.4 - 3.3 Å |
| Structure data | ![]() PDB-6p9u: ![]() PDB-6px5: |
| Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-NAG: ![]() ChemComp-HOH: ![]() ChemComp-0G6: ![]() ChemComp-NA: |
| Source |
|
Keywords | HYDROLASE / Trypsin-like protease / Allosteric equilibrium / Closed and Open conformations / hydrolase/hydrolase inhibitor / Serine protease / inhibitor / hydrolase-hydrolase inhibitor complex |
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