1brc Summary

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RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET OF TRYPSIN

The structure was published by Perona, J.J., Tsu, C.A., McGrath, M.E., Craik, C.S., and Fletterick, R.J., in 1993 in a paper entitled "Relocating a negative charge in the binding pocket of trypsin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1992.

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

This PDB entry contains a complex of 2 biomacromolecules, namely TRYPSIN and AMYLOID BETA-PROTEIN PRECURSOR INHIBITOR DOMAIN (APPI).

The molecule most likely forms heterodimers.

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
E TRYPSIN P00763 (24-246) (TRY2_RAT)search Rattus norvegicussearch 94% 223 100%
I AMYLOID BETA-PROTEIN PRECURSOR INHIBITOR DOMAIN (APPI) P05067 (287-342) (A4_HUMAN)search Homo sapienssearch < 90% 56 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P00763 (24 - 246) TRYPSIN Rattus norvegicus
P05067 (287 - 342) AMYLOID BETA-PROTEIN PRECURSOR INHIBITOR DOMAIN (APPI)

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
E (P00763) Eukaryotic proteasessearch Trypsin-like serine proteasessearch PF00089: Trypsinsearch
I Small Kunitz-type inhibitors & BPTI-like toxinssearch Factor Xa Inhibitorsearch Kunitz/Bovine pancreatic trypsin inhibitor domainsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
E (P00763) digestionsearch proteolysissearch response to nutrientsearch collagen catabolic processsearch catalytic activitysearch serine-type endopeptidase activitysearch protein bindingsearch metal ion bindingsearch calcium ion bindingsearch serine-type peptidase activitysearch hydrolase activitysearch peptidase activitysearch extracellular regionsearch extracellular spacesearch cellular_componentsearch

Chain InterPro annotation
E Peptidase S1search Peptidase S1A, chymotrypsin-typesearch Trypsin-like cysteine/serine peptidase domainsearch Peptidase S1, trypsin family, active sitesearch
I Proteinase inhibitor I2, Kunitz metazoasearch Proteinase inhibitor I2, Kunitz, conserved sitesearch