1odx Summary


HIV-1 Proteinase mutant A71T, V82A

The structure was published by Kervinen, J., Thanki, N., Zdanov, A., et al., Riccardi, K., Samanta, H., and Wlodawer, A., in 1996 in a paper entitled "Structural Analysis of the Native and Drug-Resistant HIV-1 Proteinases Complexed with an Aminodiol Inhibitor" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1996.

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 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 Biological process (GO) Molecular function (GO)
A, B (P04585) 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