1qbr Summary

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HIV-1 PROTEASE INHIBITORS WIIH LOW NANOMOLAR POTENCY

The structure was published by Jadhav, P.K., Ala, P., Woerner, F.J., et al., Garber, S.S., Anton, E.D., and Bacheler, L.T., in 1997 in a paper entitled "Cyclic urea amides: HIV-1 protease inhibitors with low nanomolar potency against both wild type and protease inhibitor resistant mutants of HIV." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1997.

The experimental data on which the structure is based was not 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 P04585 (489-587) (POL_HV1H2)search HIV-1 M:B_HXB2Rsearch < 90% 99 100%
B HIV-1 PROTEASE P04585 (489-587) (POL_HV1H2)search HIV-1 M:B_HXB2Rsearch < 90% 99 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04585 (489 - 587) HIV-1 PROTEASE Human immunodeficiency virus 1

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Retroviral protease (retropepsin)search Acid Proteasessearch Retroviral aspartyl proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P04585) aspartic-type endopeptidase activitysearch proteolysissearch

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