1NH0
1.03 A structure of HIV-1 protease: inhibitor binding inside and outside the active site
Summary for 1NH0
| Entry DOI | 10.2210/pdb1nh0/pdb |
| Related PRD ID | PRD_000401 |
| Descriptor | PROTEASE RETROPEPSIN, peptidomimetic inhibitor KI2-PHE-GLU-GLU-NH2, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | aspartyl protease, human immunodeficiency virus, inhibitor design, 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 | 4 |
| Total formula weight | 23421.42 |
| Authors | Brynda, J.,Rezacova, P.,Fabry, M.,Horejsi, M.,Hradilek, M.,Soucek, M.,Konvalinka, J.,Sedlacek, J. (deposition date: 2002-12-18, release date: 2004-04-13, Last modification date: 2023-08-16) |
| Primary citation | Brynda, J.,Rezacova, P.,Fabry, M.,Horejsi, M.,Stouracova, R.,Sedlacek, J.,Soucek, M.,Hradilek, M.,Lepsik, M.,Konvalinka, J. A Phenylnorstatine Inhibitor Binding to HIV-1 Protease: Geometry, Protonation, and Subsite-Pocket Interactions Analyzed at Atomic Resolution J.Med.Chem., 47:2030-2036, 2004 Cited by PubMed Abstract: The X-ray structure of a complex of HIV-1 protease (PR) with a phenylnorstatine inhibitor Z-Pns-Phe-Glu-Glu-NH(2) has been determined at 1.03 A, the highest resolution so far reported for any HIV PR complex. The inhibitor shows subnanomolar K(i) values for both the wild-type PR and the variant representing one of the most common mutations linked to resistance development. The structure comprising the phenylnorstatine moiety of (2R,3S)-chirality displays a unique pattern of hydrogen bonding to the two catalytic aspartate residues. This high resolution makes it possible to assess the donor and acceptor relations of this hydrogen bonding and to indicate a proton shared by the two catalytic residues. A structural mechanism for the unimpaired inhibition of the protease Val82Ala mutant is also suggested, based on energy calculations and analyses. PubMed: 15056001DOI: 10.1021/jm031105q PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.03 Å) |
Structure validation
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