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1EC0

HIV-1 protease in complex with the inhibitor bea403

Summary for 1EC0
Entry DOI10.2210/pdb1ec0/pdb
Related1AJV 1AJX 1D4H 1D4I 1D4J 1EBW 1EBY 1EBZ 1EC1 1EC2 1EC3
DescriptorHIV-1 PROTEASE, N,N-[2,5-O-DI-2-FLUORO-BENZYL-GLUCARYL]-DI-[1-AMINO-INDAN-2-OL] (3 entities in total)
Functional Keywordsdimer, protein-inhibitor complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHuman immunodeficiency virus 1
Cellular locationGag-Pol polyprotein: Host cell membrane; Lipid-anchor. Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P03366
Total number of polymer chains2
Total formula weight22296.23
Authors
Unge, T. (deposition date: 2000-01-25, release date: 2002-06-26, Last modification date: 2024-02-07)
Primary citationLindberg, J.,Pyring, D.,Lowgren, S.,Rosenquist, A.,Zuccarello, G.,Kvarnstrom, I.,Zhang, H.,Vrang, L.,Classon, B.,Hallberg, A.,Samuelsson, B.,Unge, T.
Symmetric fluoro-substituted diol-based HIV protease inhibitors. Ortho-fluorinated and meta-fluorinated P1/P1'-benzyloxy side groups significantly improve the antiviral activity and preserve binding efficacy
Eur.J.Biochem., 271:4594-4602, 2004
Cited by
PubMed: 15560801
DOI: 10.1111/j.1432-1033.2004.04431.x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.79 Å)
Structure validation

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