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3UFN

Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical Isolate PR20 in Complex with Saquinavir

Summary for 3UFN
Entry DOI10.2210/pdb3ufn/pdb
Related3UCB 3UF3 3UHL
Related PRD IDPRD_000454
DescriptorHIV-1 protease, (2S)-N-[(2S,3R)-4-[(2S,3S,4aS,8aS)-3-(tert-butylcarbamoyl)-3,4,4a,5,6,7,8,8a-octahydro-1H-isoquinolin-2-yl]-3-hydroxy-1 -phenyl-butan-2-yl]-2-(quinolin-2-ylcarbonylamino)butanediamide, CHLORIDE ION, ... (4 entities in total)
Functional Keywordshydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHomo sapiens (human)
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): P03367
Total number of polymer chains2
Total formula weight22945.67
Authors
Agniswamy, J.,Chen-Hsiang, S.,Aniana, A.,Sayer, J.M.,Louis, J.M.,Weber, I.T. (deposition date: 2011-11-01, release date: 2012-03-28, Last modification date: 2024-02-28)
Primary citationAgniswamy, J.,Shen, C.H.,Aniana, A.,Sayer, J.M.,Louis, J.M.,Weber, I.T.
HIV-1 protease with 20 mutations exhibits extreme resistance to clinical inhibitors through coordinated structural rearrangements.
Biochemistry, 51:2819-2828, 2012
Cited by
PubMed: 22404139
DOI: 10.1021/bi2018317
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

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