Structure of PDB 5wob Chain F Binding Site BS02

Receptor Information
>5wob Chain F (length=944) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVH
IGSLSDPPNIAGLSHFLQHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTS
GEHTNYYFDVSHEHLEGALDRFAQFFLSPLFDEKDREVNAVDSEHEKNVM
NDAWRLFQLEKATGNPKHPFSKFGTGNKYTLTRPNQEGIDVRQELLKFHS
AYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEE
HLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSL
LSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQ
YIQKLRAEGPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILHYYPL
EEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWY
GTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATP
YPALIKDTAMSKLWFKQDDKFLPKANLNFEFFSPFAYVDPLHSNMAYLYL
ELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIE
KMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTK
DELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVED
TLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNGIEIYYQTD
MQSTSENMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGIQGLRF
IIQSEKPPHYLESRVEAFLITMEKSIETEFQKHIQALAIRRLDKPKKLSA
ESAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDPRRHK
VSVHVLAREMINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPH
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain5wob Chain F Residue 1101 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5wob Ensemble cryoEM elucidates the mechanism of insulin capture and degradation by human insulin degrading enzyme.
Resolution3.95 Å
Binding residue
(original residue number in PDB)
H108 H112 E189
Binding residue
(residue number reindexed from 1)
H65 H69 E144
Annotation score4
Enzymatic activity
Enzyme Commision number 3.4.24.56: insulysin.
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

View graph for
Cellular Component
External links
PDB RCSB:5wob, PDBe:5wob, PDBj:5wob
PDBsum5wob
PubMed29596046
UniProtP14735|IDE_HUMAN Insulin-degrading enzyme (Gene Name=IDE)

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