4k4q Summary


TL-3 inhibited Trp6Ala HIV Protease with 3-bromo-2,6-dimethoxybenzoic acid bound in flap site

The structure was published by Tiefenbrunn, T., Forli, S., Happer, M., et al., Elder, J.H., Olson, A.J., and Stout, C.D., in 2014 in a paper entitled "Crystallographic Fragment-Based Drug Discovery: Use of a Brominated Fragment Library Targeting HIV Protease." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2013.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of HIV-1 protease.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A HIV-1 protease P12499 (490-588) (POL_HV1Z2)search Human immunodeficiency virus type 1 (Z2/CDC-Z34 ISOLATE)search < 90% 99 100%
B HIV-1 protease P12499 (490-588) (POL_HV1Z2)search Human immunodeficiency virus type 1 (Z2/CDC-Z34 ISOLATE)search < 90% 99 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P12499 (490 - 588) HIV-1 protease Human immunodeficiency virus type 1 (Z2/CDC-Z34 ISOLATE)

Chain Sequence family (Pfam)
A, B Retroviral aspartyl proteasesearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (P12499) proteolysissearch aspartic-type endopeptidase activitysearch

Chain InterPro annotation
A, B Aspartic peptidase, active sitesearch Peptidase A2A, retrovirus, catalyticsearch Peptidase A2A, retrovirus RVP subgroupsearch Aspartic peptidase domainsearch