+Search query
-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 |