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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

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 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.47 HIV-2 retropepsin

Crystallization

Crystallization on EC 3.4.23.47 - HIV-2 retropepsin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamics simulations in complerx with inhibitors amprenvir and darunavir
analysis of 19 ligand-bound wild-type enzyme crystal structures, overview. Mutation K57L is experimentally introduced in 8 structures to help the crystallographic process
crystallized by hanging drop method in complex with a reduced amide inhibitor, BI-LA-398
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crystals grown by hanging-drop vapor diffusion method, thin tetragonal prisms, space group P4(1)2(1)2 or P4(3)2(1)2 with a=b=62.6 A and c=115.8 A
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in complex with inhibitor amprenavir, to 1.5 A resolution, and comparison with HIV-1 protease PR1M
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monoclinic crystals, vapor diffusion, hanging drops, P2(1) space group with a =36.76 A, b=58.44 A, c= 55.11 A and beta=91.20°
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Phe-Val-Phe-psi-CH2NH-Leu-Glu-Ile-amide, space group P4(1) or P4(3), unit-cell parameters a=b=55.1 A, c=138.9 A
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substrate binding pocket structure analysis
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