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| Title | Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution. |
|---|---|
| Journal, issue, pages | J. Biol. Chem., Vol. 285, Page 34039-34047, Year 2010 |
| Publish date | Jan 20, 2010 (structure data deposition date) |
Authors | Sohn, J. / Grant, R.A. / Sauer, R.T. |
External links | J. Biol. Chem. / PubMed:20739286 |
| Methods | X-ray diffraction |
| Resolution | 1.652 - 2.734 Å |
| Structure data | ![]() PDB-3lgi: ![]() PDB-3lgt: ![]() PDB-3lgu: ![]() PDB-3lgv: ![]() PDB-3lgw: ![]() PDB-3lgy: ![]() PDB-3lh1: ![]() PDB-3lh3: |
| Chemicals | ![]() ChemComp-PO4: ![]() ChemComp-HOH: ![]() ChemComp-CL: ![]() ChemComp-MG: |
| Source |
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Keywords | HYDROLASE / protease / stress-sensor / HtrA / PDZ OMP / Serine protease |
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