1IDA
CRYSTAL STRUCTURES OF HIV-2 PROTEASE IN COMPLEX WITH INHIBITORS CONTAINING THE HYDROXYETHYLAMINE DIPEPTIDE ISOSTERE
Summary for 1IDA
Entry DOI | 10.2210/pdb1ida/pdb |
Related | 1IDB |
Related PRD ID | PRD_000340 |
Descriptor | Protease, N-[(1R)-1-{[(1S,2S)-1-benzyl-3-{(2R,4S)-2-(tert-butylcarbamoyl)-4-[(pyridin-3-ylmethyl)sulfanyl]piperidin-1-yl}-2-hydroxypropyl]carbamoyl}-2-methylpropyl]quinoline-2-carboxamide (3 entities in total) |
Functional Keywords | acid proteinase, aids, protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Human immunodeficiency virus type 2 (HIV-2) |
Total number of polymer chains | 2 |
Total formula weight | 22181.63 |
Authors | Tong, L.,Anderson, P.C. (deposition date: 1994-10-19, release date: 1995-01-26, Last modification date: 2024-02-07) |
Primary citation | Tong, L.,Pav, S.,Mui, S.,Lamarre, D.,Yoakim, C.,Beaulieu, P.,Anderson, P.C. Crystal structures of HIV-2 protease in complex with inhibitors containing the hydroxyethylamine dipeptide isostere. Structure, 3:33-40, 1995 Cited by PubMed Abstract: The HIV protease is essential for the life cycle of the virus and is an important target for the development of therapeutic treatments against AIDS. The structures of HIV protease in complex with different inhibitors have helped in understanding the interactions between inhibitors and the protease and in the design and optimization of HIV protease inhibitors. PubMed: 7743130DOI: 10.1016/S0969-2126(01)00133-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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