1ebz Summary


HIV-1 protease in complex with the inhibitor BEA388

The structure was published by Andersson, H.O., Fridborg, K., Lowgren, S., et al., Samuelsson, B., Hallberg, A., and Unge, T., in 2003 in a paper entitled "Optimization of P1-P3 groups in symmetric and asymmetric HIV-1 protease inhibitors" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.01 Å and deposited in 2000.

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 P03366 (501-599) (POL_HV1B1)search Human immunodeficiency virus type 1 BH10search < 90% 99 100%
B HIV-1 PROTEASE P03366 (501-599) (POL_HV1B1)search Human immunodeficiency virus type 1 BH10search < 90% 99 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P03366 (501 - 599) 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 (P03366) 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