1a30 Summary

pdbe.org/1a30
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HIV-1 PROTEASE COMPLEXED WITH A TRIPEPTIDE INHIBITOR

The structure was published by Louis, J.M., Dyda, F., Nashed, N.T., Kimmel, A.R., and Davies, D.R., in 1998 in a paper entitled "Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1998.

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

This PDB entry contains a complex of 2 biomacromolecules, namely HIV-1 PROTEASE and TRIPEPTIDE GLU-ASP-LEU.

The molecule most likely forms heterotrimers.

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%
C TRIPEPTIDE GLU-ASP-LEU Not available
Not available Not available 3 100%


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
C

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
C