1HHP: The Three-Dimensional Structure Of The Aspartyl Protease From The Hiv- 1 Isolate Bru

The crystal structure of the aspartyl protease encoded by the gene pol of the human immunodeficiency virus (HIV-1, isolate BRU) has been determined to 2.7 A resolution. The enzyme, expressed as an insoluble denatured polypeptide in inclusion bodies of Escherichia coli has been renatured and crystallized. It differs by several amino acid replacements from the homologous enzymes of other HIV-1 isolates. A superposition of the C alpha-backbone of the BRU protease with that of the SF2 protease gives a roots mean square positional difference of 0.45 A. Thus, neither the denaturation/renaturation process nor the amino acid replacements have a noticeable effect on the three-dimensional structure of the BRU protease or on the detailed conformation of the catalytic site, which is very similar to that of other aspartyl proteases.
PDB ID: 1HHPDownload
MMDB ID: 56338
PDB Deposition Date: 1992/5/27
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 1HHP: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 1HHP
Label Count Molecule
Proteins (2 molecules)
Unliganded Hiv-1 Protease
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB