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3CYW

Effect of Flap Mutations on Structure of HIV-1 Protease and Inhibition by Saquinavir and Darunavir

Summary for 3CYW
Entry DOI10.2210/pdb3cyw/pdb
Related3CYX
DescriptorHIV-1 Protease, CHLORIDE ION, (3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE, ... (5 entities in total)
Functional Keywordsdrug resistance; hiv-1, aids, aspartyl protease, capsid maturation, capsid protein, dna integration, dna recombination, dna-directed dna polymerase, endonuclease, hydrolase, lipoprotein, magnesium, membrane, metal-binding, multifunctional enzyme, myristate, nuclease, nucleotidyltransferase, nucleus, phosphoprotein, protease, rna-binding, rna-directed dna polymerase, transferase, viral nucleoprotein, virion, zinc-finger
Biological sourceHuman immunodeficiency virus type 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): P04587
Total number of polymer chains2
Total formula weight22382.53
Authors
Liu, F.,Weber, I.T. (deposition date: 2008-04-27, release date: 2008-05-27, Last modification date: 2023-08-30)
Primary citationLiu, F.,Kovalevsky, A.Y.,Tie, Y.,Ghosh, A.K.,Harrison, R.W.,Weber, I.T.
Effect of flap mutations on structure of HIV-1 protease and inhibition by saquinavir and darunavir.
J.Mol.Biol., 381:102-115, 2008
Cited by
PubMed: 18597780
DOI: 10.1016/j.jmb.2008.05.062
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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