Structure of PDB 7rzi Chain A

Receptor sequence
>7rziA (length=948) Species: 9606 (Homo sapiens) [Search protein sequence]
IKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGS
LSDPPNIAGLSHFLEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEH
TNYYFDVSHEHLEGALDRFAQFFLSPLFDESAKDREVNAVDSEHEKNVMN
DAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHS
AYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEE
HLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSL
LSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQ
YIQKLRAEGPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILHYYPL
EEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWY
GTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATP
YPALIKDTAMSKLWFKQDDKFFLPKANLNFEFFSPFAYVDPLHSNMAYLY
LELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKII
EKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWT
KDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVE
DTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNSGIEIYYQ
TDMQSTSENMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGIQGL
RFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDK
PKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAV
DAPRRHKVSVHVLAREMSQAPALPQPEVIQNMTEFKRGLPLFPLVKPH
3D structure
PDB7rzi Ensemble cryoEM reveals a substrate-induced shift in the conformational dynamics of human insulin degrading enzyme
ChainA
Resolution3.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.24.56: insulysin.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 peptide A H108 H112 F115 N139 A140 F141 Y150 E189 W199 R431 G432 F820 Y831 H62 H66 F69 N93 A94 F95 Y104 E143 W153 R385 G386 F774 Y785
BS02 peptide A G335 G339 V360 G361 Q363 E365 G289 G293 V314 G315 Q317 E319
Gene Ontology
Molecular Function
GO:0001618 virus receptor activity
GO:0004175 endopeptidase activity
GO:0004222 metalloendopeptidase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0042277 peptide binding
GO:0042803 protein homodimerization activity
GO:0043559 insulin binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0008286 insulin receptor signaling pathway
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:0032092 positive regulation of protein binding
GO:0042447 hormone catabolic process
GO:0043171 peptide catabolic process
GO:0045732 positive regulation of protein catabolic process
GO:0046718 symbiont entry into host cell
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:0070062 extracellular exosome

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7rzi, PDBe:7rzi, PDBj:7rzi
PDBsum7rzi
PubMed
UniProtP14735|IDE_HUMAN Insulin-degrading enzyme (Gene Name=IDE)

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