1HEG

The crystal structures at 2.2 angstroms resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations

Summary for 1HEG

Entry DOI	10.2210/pdb1heg/pdb
Related PRD ID	PRD_000320
Descriptor	HIV-1 PROTEASE, methyl N-{(4S,5S)-5-[(L-alanyl-L-alanyl)amino]-4-hydroxy-6-phenylhexanoyl}-L-valyl-L-valinate (3 entities in total)
Functional Keywords	hydrolase-hydrolase inhibitor complex, acid proteinase, hydrolase/hydrolase inhibitor
Biological source	Human immunodeficiency virus 1
Cellular location	Gag-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 chains	1
Total formula weight	11364.38
Authors	Murthy, K.,Winborne, E.L.,Minnich, M.D.,Culp, J.S.,Debouck, C. (deposition date: 1992-09-21, release date: 1994-05-31, Last modification date: 2024-03-13)
Primary citation	Murthy, K.H.,Winborne, E.L.,Minnich, M.D.,Culp, J.S.,Debouck, C. The crystal structures at 2.2-A resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations. J.Biol.Chem., 267:22770-22778, 1992 Cited by PubMed: 1429626 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation