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TitleNon-active site mutations in the HIV protease: Diminished drug binding affinity is achieved through modulating the hydrophobic sliding mechanism.
Journal, issue, pagesInt. J. Biol. Macromol., Vol. 217, Page 27-41, Year 2022
Publish dateNov 9, 2018 (structure data deposition date)
AuthorsSherry, D. / Pandian, R. / Sayed, Y.
External linksInt. J. Biol. Macromol. / PubMed:35817239
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-6i45:
Crystal structure of I13V/I62V/V77I South African HIV-1 subtype C protease containing a D25A mutation
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • human immunodeficiency virus 1
KeywordsHYDROLASE / HIV / AIDS / Human / Protease / apo

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