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Structure paper

TitleHighly conserved glycine 86 and arginine 87 residues contribute differently to the structure and activity of the mature HIV-1 protease
Journal, issue, pagesProteins, Vol. 78, Page 1015-1025, Year 2009
Publish dateSep 17, 2009 (structure data deposition date)
AuthorsIshima, R. / Gong, Q. / Tie, Y. / Weber, I.T. / Louis, J.M.
External linksProteins / PubMed:19899162
MethodsX-ray diffraction
Resolution1.6 - 1.8 Å
Structure data

PDB-3jvw:
HIV-1 Protease Mutant G86A with symmetric inhibitor DMP323
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3jvy:
HIV-1 Protease Mutant G86A with DARUNAVIR
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-3jw2:
HIV-1 Protease Mutant G86S with DARUNAVIR
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-DMP:
[4-R-(-4-ALPHA,5-ALPHA,6-BETA,7-BETA)]-HEXAHYDRO-5,6-BIS(HYDROXY)-[1,3-BIS([4-HYDROXYMETHYL-PHENYL]METHYL)-4,7-BIS(PHEN

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-017:
(3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE / medication, antiretroviral*YM

Source
  • human immunodeficiency virus type 1 (bru isolate)
KeywordsHYDROLASE / HIV-1 Protease / Mutant G86A / symmetric inhibitor / DMP323 / AIDS / Aspartyl protease / INHIBITOR / DARUNAVIR / METAL-BINDING / Mutant G86S

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