3NU5
Crystal Structure of HIV-1 Protease Mutant I50V with Antiviral Drug Amprenavir
Summary for 3NU5
Entry DOI | 10.2210/pdb3nu5/pdb |
Related | 2IEN 3NU3 3NU4 3NU6 3NU9 3NUJ 3NUO |
Descriptor | protease, SODIUM ION, CHLORIDE ION, ... (6 entities in total) |
Functional Keywords | enzyme inhibition, aspartic protease, hiv/aids, conformational change, amprenavir, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Human immunodeficiency virus 1 |
Cellular location | Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P03366 |
Total number of polymer chains | 2 |
Total formula weight | 22394.15 |
Authors | Wang, Y.-F.,Shen, C.H.,Weber, I.T. (deposition date: 2010-07-06, release date: 2010-08-25, Last modification date: 2023-09-06) |
Primary citation | Shen, C.H.,Wang, Y.F.,Kovalevsky, A.Y.,Harrison, R.W.,Weber, I.T. Amprenavir complexes with HIV-1 protease and its drug-resistant mutants altering hydrophobic clusters. Febs J., 277:3699-3714, 2010 Cited by PubMed: 20695887DOI: 10.1111/j.1742-4658.2010.07771.x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.29 Å) |
Structure validation
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