1HPX
HIV-1 PROTEASE COMPLEXED WITH THE INHIBITOR KNI-272
Summary for 1HPX
Entry DOI | 10.2210/pdb1hpx/pdb |
Related PRD ID | PRD_000562 |
Descriptor | HIV-1 PROTEASE, (4R)-N-tert-butyl-3-[(2S,3S)-2-hydroxy-3-({N-[(isoquinolin-5-yloxy)acetyl]-S-methyl-L-cysteinyl}amino)-4-phenylbutanoyl]-1,3-thiazolidine-4-carboxamide (3 entities in total) |
Functional Keywords | acid protease, hydrolase, 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): P03367 |
Total number of polymer chains | 2 |
Total formula weight | 22275.35 |
Authors | Bhat, T.N.,Erickson, J.W. (deposition date: 1995-05-18, release date: 1996-03-08, Last modification date: 2024-02-07) |
Primary citation | Baldwin, E.T.,Bhat, T.N.,Gulnik, S.,Liu, B.,Topol, I.A.,Kiso, Y.,Mimoto, T.,Mitsuya, H.,Erickson, J.W. Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine. Structure, 3:581-590, 1995 Cited by PubMed: 8590019DOI: 10.1016/S0969-2126(01)00192-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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