1bve Summary

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HIV-1 PROTEASE-DMP323 COMPLEX IN SOLUTION, NMR, 28 STRUCTURES

The structure was published by Yamazaki, T., Hinck, A.P., Wang, Y.X., et al., Chang, C.H., Domaille, P.J., and Lam, P.Y., in 1996 in a paper entitled "Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy." (abstract).

The structure was determined using NMR spectroscopy 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 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