3.4.23.47: HIV-2 retropepsin
This is an abbreviated version!
For detailed information about HIV-2 retropepsin, go to the full flat file.
Word Map on EC 3.4.23.47
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3.4.23.47
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polyproteins
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antiretroviral
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medicine
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darunavir
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saquinavir
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amprenavir
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lopinavir
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myeloblastosis
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nelfinavir
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hiv-2-infected
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drv
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drug development
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molecular biology
- 3.4.23.47
- polyproteins
-
antiretroviral
- medicine
- darunavir
- saquinavir
- amprenavir
- lopinavir
-
myeloblastosis
- nelfinavir
-
hiv-2-infected
- drv
- drug development
- molecular biology
Reaction
Endopeptidase for which the P1 residue is preferably hydrophobic =
Synonyms
HIV-2 protease, HIV-2 proteinase, human immunodeficiency virus 2 retropepsin, More, PR, PR2, retroviral aspartic proteinase, retroviral proteinase
ECTree
3.4.23.47 HIV-2 retropepsinAdvanced search results
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General Information on EC 3.4.23.47 - HIV-2 retropepsin
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
HIV proteases PR1 and PR2 share only approximately 50% of sequence identity but they exhibit a similar global fold
physiological function
HIV PR2 is essential for hydrolysing the viral Gag and the Gag-Pol precursor polyproteins during the maturation of infectious viral particles
additional information
additional information
77% of PR2 positions are structurally variable, meaning they exhibit different local conformations in PR2 structures, structural variability of the binding pocket and PR2-ligand interactions, ligand binding structure analysis, detailed overview. The catalytic position is D25A/B
additional information
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77% of PR2 positions are structurally variable, meaning they exhibit different local conformations in PR2 structures, structural variability of the binding pocket and PR2-ligand interactions, ligand binding structure analysis, detailed overview. The catalytic position is D25A/B
additional information
comparison of the HIV-1 protease and HIV-2 protease binding pockets extracted from structures complexed with 12 ligands, overview
additional information
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comparison of the HIV-1 protease and HIV-2 protease binding pockets extracted from structures complexed with 12 ligands, overview
additional information
PR2 is an aspartic protease corresponding to a C2-symmetric homodimer of 99 residues in each monomer. The ligand binding site is located at the interface between the two monomers and includes the catalytic triplet, Asp-Thr-Gly, conserved in all aspartic proteases. Detection of structural local asymmetry in the PR2 dimer complexed with a diversified set of ligands, global structural asymmetry of PR2 dimers, overview
additional information
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PR2 is an aspartic protease corresponding to a C2-symmetric homodimer of 99 residues in each monomer. The ligand binding site is located at the interface between the two monomers and includes the catalytic triplet, Asp-Thr-Gly, conserved in all aspartic proteases. Detection of structural local asymmetry in the PR2 dimer complexed with a diversified set of ligands, global structural asymmetry of PR2 dimers, overview
