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3NU5

Crystal Structure of HIV-1 Protease Mutant I50V with Antiviral Drug Amprenavir

Summary for 3NU5
Entry DOI10.2210/pdb3nu5/pdb
Related2IEN 3NU3 3NU4 3NU6 3NU9 3NUJ 3NUO
Descriptorprotease, SODIUM ION, CHLORIDE ION, ... (6 entities in total)
Functional Keywordsenzyme inhibition, aspartic protease, hiv/aids, conformational change, amprenavir, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHuman immunodeficiency virus 1
Cellular locationMatrix 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 chains2
Total formula weight22394.15
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 citationShen, 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: 20695887
DOI: 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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