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-Structure paper
Title | The L76V Drug Resistance Mutation Decreases the Dimer Stability and Rate of Autoprocessing of HIV-1 Protease by Reducing Internal Hydrophobic Contacts. |
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Journal, issue, pages | Biochemistry, Vol. 50, Page 4786-4795, Year 2011 |
Publish date | Dec 8, 2010 (structure data deposition date) |
![]() | Louis, J.M. / Zhang, Y. / Sayer, J.M. / Wang, Y.F. / Harrison, R.W. / Weber, I.T. |
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Methods | X-ray diffraction |
Resolution | 1.45 - 1.46 Å |
Structure data | ![]() PDB-3pwm: ![]() PDB-3pwr: |
Chemicals | ![]() ChemComp-CL: ![]() ChemComp-ACT: ![]() ChemComp-NA: ![]() ChemComp-017: ![]() ChemComp-HOH: ![]() ChemComp-ROC: ![]() ChemComp-GOL: |
Source |
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![]() | HYDROLASE/HYDROLASE INHIBITOR / HIV-1 / protease / mutation L76V / darunavir / HYDROLASE / HYDROLASE-HYDROLASE INHIBITOR complex / saquinavir |