3phv Summary

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X-RAY ANALYSIS OF HIV-1 PROTEINASE AT 2.7 ANGSTROMS RESOLUTION CONFIRMS STRUCTURAL HOMOLOGY AMONG RETROVIRAL ENZYMES

The structure was published by Lapatto, R., Blundell, T., Hemmings, A., et al., Lee, S.E., Scheld, K.G., and Hobart, P.M., in 1989 in a paper entitled "X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 1991.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of UNLIGANDED HIV-1 PROTEASE. This molecule has the UniProt identifier P04585 (POL_HV1H2)search. The sample contained 99 residues which is < 90% of the natural sequence. Out of 99 residues 99 were observed and are deposited in the PDB.

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 UNLIGANDED 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) UNLIGANDED HIV-1 PROTEASE HIV-1 M:B_HXB2R

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