Structure of PDB 3p7o Chain A Binding Site BS02

Receptor Information
>3p7o Chain A (length=958) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MNNPAIQRIEDHIVKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALD
VHIGSLSDPPNIPGLSHFCFHMLFLGTKKYPKENEYSQFLSEHAGSSNAF
TSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDASCKDREVNAVDSEHE
KNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVREEL
LKFHSTYYSSNLMAICVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEH
PFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQQYYKSNPGHYLGHLIGHE
GPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDII
LHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGKL
HYYPLNGVLTAEYLLEEFRPDLIDMVLDKLRPENVRVAIVSKSFEGKTDR
TEQWYGTQYKQEAIPEDVIQKWQNADLNGKFKLPTKNEFIPTNFEILALE
KDATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCN
MAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPIL
LKKITEKMATFEIDKKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMT
EVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGV
MQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQRRNEVHNNCGI
EIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRAN
GIQGLRFIIQSEKPPHYLESRVEAFLITMEKAIEDMTEEAFQKHIQALAI
RRLDKPKKLSAECAKYWGEIISQQYNYDRDNIEVAYLKTLSKDDIIKFYK
EMLAVDAPRRHKVSVHVLAREMDSINLSEAPPLPQPEVIHNMTEFKRGLP
LFPLVKPH
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3p7o Identification of the allosteric regulatory site of insulysin.
Resolution2.1423 Å
Binding residue
(original residue number in PDB)		H332 G339 E341 L359 V360 G361 Y609
Binding residue
(residue number reindexed from 1)		H291 G298 E300 L318 V319 G320 Y568
Enzymatic activity
Enzyme Commision number 3.4.24.56: insulysin.
Gene Ontology
Molecular Function
GO:0001540 amyloid-beta binding
GO:0004175 endopeptidase activity
GO:0004222 metalloendopeptidase activity
GO:0005524 ATP binding
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0016887 ATP hydrolysis activity
GO:0017046 peptide hormone binding
GO:0031626 beta-endorphin binding
GO:0042277 peptide binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0043559 insulin binding
GO:0044877 protein-containing complex binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0006979 response to oxidative stress
GO:0010815 bradykinin catabolic process
GO:0010992 ubiquitin recycling
GO:0019885 antigen processing and presentation of endogenous peptide antigen via MHC class I
GO:0030163 protein catabolic process
GO:0038020 insulin receptor recycling
GO:0042447 hormone catabolic process
GO:0043171 peptide catabolic process
GO:0045861 negative regulation of proteolysis
GO:0050435 amyloid-beta metabolic process
GO:0051603 proteolysis involved in protein catabolic process
GO:0097242 amyloid-beta clearance
GO:0150094 amyloid-beta clearance by cellular catabolic process
GO:1901142 insulin metabolic process
GO:1901143 insulin catabolic process
GO:1903715 regulation of aerobic respiration
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005777 peroxisome
GO:0005782 peroxisomal matrix
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009897 external side of plasma membrane
GO:0009986 cell surface
GO:0016323 basolateral plasma membrane
GO:0031597 cytosolic proteasome complex
GO:0031904 endosome lumen
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3p7o, PDBe:3p7o, PDBj:3p7o
PDBsum3p7o
PubMed21731629
UniProtP35559|IDE_RAT Insulin-degrading enzyme (Gene Name=Ide)

[Back to BioLiP]