4ID5: HIV-1 reverse transcriptase with bound fragment at the RNase H primer grip site

Citation:
Abstract
HIV-1 reverse transcriptase (RT) undergoes a series of conformational changes during viral replication and is a central target for antiretroviral therapy. The intrinsic flexibility of RT can provide novel allosteric sites for inhibition. Crystals of RT that diffract X-rays to better than 2 A resolution facilitated the probing of RT for new druggable sites using fragment screening by X-ray crystallography. A total of 775 fragments were grouped into 143 cocktails, which were soaked into crystals of RT in complex with the non-nucleoside drug rilpivirine (TMC278). Seven new sites were discovered, including the Incoming Nucleotide Binding, Knuckles, NNRTI Adjacent, and 399 sites, located in the polymerase region of RT, and the 428, RNase H Primer Grip Adjacent, and 507 sites, located in the RNase H region. Three of these sites (Knuckles, NNRTI Adjacent, and Incoming Nucleotide Binding) are inhibitory and provide opportunities for discovery of new anti-AIDS drugs.
PDB ID: 4ID5Download
MMDB ID: 107362
PDB Deposition Date: 2012/12/11
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.95  Å
Source Organism:
Similar Structures:
Biological Unit for 4ID5: dimeric; determined by author and by software (PISA)
Molecular Components in 4ID5
Label Count Molecule
Proteins (2 molecules)
1
Reverse Transcriptase/ribonuclease H
Molecule annotation
1
P51 RT
Molecule annotation
Chemicals (20 molecules)
1
1
2
17
3
1
4
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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