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X-RAY ANALYSES OF PEPTIDE INHIBITOR COMPLEXES DEFINE THE STRUCTURAL BASIS OF SPECIFICITY FOR HUMAN AND MOUSE RENINS

The structure was published by Dhanaraj, V., Dealwis, C.G., Frazao, C., et al., Geoghegan, K.F., Ammirati, M.J., and Danley, D.E., in 1992 in a paper entitled "X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 1992.

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

This PDB entry contains multiple copies of the structure of RENIN.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 RENIN P00797 (67-406) (RENI_HUMAN)search Homo sapienssearch 100% 340 97%
B RENIN P00797 (67-406) (RENI_HUMAN)search Homo sapienssearch 100% 340 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00797 (67 - 406) RENIN Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P00797) Pepsin-likesearch Acid Proteasessearch PF00026: Eukaryotic aspartyl proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P00797) aspartic-type endopeptidase activitysearch proteolysissearch

Chain InterPro annotation
A, B Aspartic peptidasesearch Aspartic peptidase, active sitesearch Aspartic peptidase domainsearch