1lv1 Summary

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Crystal Structure Analysis of the non-active site mutant of tethered HIV-1 protease to 2.1A resolution

The structure was published by Kumar, M., Kannan, K.K., Hosur, M.V., et al., Chatterjee, A., Mittal, R., and Hosur, R.V., in 2002 in a paper entitled "Effects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2002.

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

The PDB entry contains the structure of HIV-1 protease. This molecule has the UniProt identifier P04585 (POL_HV1H2)search. The sample contained 203 residues which is < 90% of the natural sequence. Out of 203 residues 197 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

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 (484-488) (POL_HV1H2)search ,
P04585 (489-587) (POL_HV1H2)search
HIV-1 M:B_HXB2Rsearch ,
HIV-1 M:B_HXB2Rsearch
< 90% ,
< 90%
203 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04585 (484 - 488) HIV-1 protease Human immunodeficiency virus 1

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

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

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