Structure of PDB 2wby Chain B Binding Site BS01

Receptor Information
>2wby Chain B (length=954) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVH
IGSLSDPPNIAGLSHFLQHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTS
GEHTNYYFDVSHEHLEGALDRFAQFFLSPLFDESAKDREVNAVDSEHEKN
VMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLK
FHSAYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPF
QEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGP
GSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILH
MFQYIQKLRAEGPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILHY
YPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTE
EWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKE
ATPYPALIKDTAMSKLWFKQDDKFFLPKANLNFEFFSPFAYVDPLHSNMA
YLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLK
KIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEV
AWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQ
MVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNSGIEI
YYQTDMQSTSENMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGI
QGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRR
LDKPKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEM
LAVDAPRRHKVSVHVLAREMDNLSQAPALPQPEVIQNMTEFKRGLPLFPL
VKPH
Ligand information
>2wby Chain E (length=20) Species: 9606 (Homo sapiens) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
GIVEQCCTSICSLYQLENYC
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2wby Molecular Basis of Catalytic Chamber-Assisted Unfolding and Cleavage of Human Insulin by Human Insulin Degrading Enzyme.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		F141 Y150 H336 G339 E341 V360 G361 G362 Q363 E365 I374 R429 R431 G432
Binding residue
(residue number reindexed from 1)		F98 Y107 H293 G296 E298 V317 G318 G319 Q320 E322 I331 R386 R388 G389
Enzymatic activity
Catalytic site (original residue number in PDB) Q111
Catalytic site (residue number reindexed from 1) Q68
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2wby, PDBe:2wby, PDBj:2wby
PDBsum2wby
PubMed19321446
UniProtP14735|IDE_HUMAN Insulin-degrading enzyme (Gene Name=IDE)

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