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-Structure paper
| Title | Flexibility of the Thrombin-activatable Fibrinolysis Inhibitor Pro-domain Enables Productive Binding of Protein Substrates. |
|---|---|
| Journal, issue, pages | J. Biol. Chem., Vol. 285, Page 38243-38250, Year 2010 |
| Publish date | Sep 9, 2010 (structure data deposition date) |
Authors | Valnickova, Z. / Sanglas, L. / Arolas, J.L. / Petersen, S.V. / Schar, C. / Otzen, D. / Aviles, F.X. / Gomis-Ruth, F.X. / Enghild, J.J. |
External links | J. Biol. Chem. / PubMed:20880845 |
| Methods | X-ray diffraction |
| Resolution | 6 Å |
| Structure data | ![]() PDB-3osl: |
| Chemicals | ![]() ChemComp-ZN: |
| Source |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / alpha/beta-hydrolase-related fold / Blood / fibrinolysis / coagulation / HYDROLASE-HYDROLASE INHIBITOR complex |
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rhipicephalus bursa (arthropod)
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