3P7O
Rat Insulin Degrading Enzyme (Insulysin) E111F mutant with two bound peptides
Summary for 3P7O
Entry DOI | 10.2210/pdb3p7o/pdb |
Descriptor | Insulin-degrading enzyme, active site bound peptide, distal site bound peptide, ... (4 entities in total) |
Functional Keywords | metallopeptidase, hydrolase |
Biological source | Rattus norvegicus (brown rat,rat,rats) More |
Cellular location | Cytoplasm: P35559 |
Total number of polymer chains | 3 |
Total formula weight | 119195.49 |
Authors | Rodgers, D.W.,Noinaj, N. (deposition date: 2010-10-12, release date: 2011-07-27, Last modification date: 2024-02-21) |
Primary citation | Noinaj, N.,Bhasin, S.K.,Song, E.S.,Scoggin, K.E.,Juliano, M.A.,Juliano, L.,Hersh, L.B.,Rodgers, D.W. Identification of the allosteric regulatory site of insulysin. Plos One, 6:e20864-e20864, 2011 Cited by PubMed Abstract: Insulin degrading enzyme (IDE) is responsible for the metabolism of insulin and plays a role in clearance of the Aβ peptide associated with Alzheimer's disease. Unlike most proteolytic enzymes, IDE, which consists of four structurally related domains and exists primarily as a dimer, exhibits allosteric kinetics, being activated by both small substrate peptides and polyphosphates such as ATP. PubMed: 21731629DOI: 10.1371/journal.pone.0020864 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1423 Å) |
Structure validation
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