Structure of PDB 2wby Chain B
Receptor sequence
>2wbyB (length=954) Species:
9606
(Homo sapiens) [
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NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVH
IGSLSDPPNIAGLSHFLQHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTS
GEHTNYYFDVSHEHLEGALDRFAQFFLSPLFDESAKDREVNAVDSEHEKN
VMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLK
FHSAYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPF
QEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGP
GSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILH
MFQYIQKLRAEGPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILHY
YPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTE
EWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKE
ATPYPALIKDTAMSKLWFKQDDKFFLPKANLNFEFFSPFAYVDPLHSNMA
YLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLK
KIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEV
AWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQ
MVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNSGIEI
YYQTDMQSTSENMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGI
QGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRR
LDKPKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEM
LAVDAPRRHKVSVHVLAREMDNLSQAPALPQPEVIQNMTEFKRGLPLFPL
VKPH
3D structure
PDB
2wby
Molecular Basis of Catalytic Chamber-Assisted Unfolding and Cleavage of Human Insulin by Human Insulin Degrading Enzyme.
Chain
B
Resolution
2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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
B
F141 Y150 H336 G339 E341 V360 G361 G362 Q363 E365 I374 R429 R431 G432
F98 Y107 H293 G296 E298 V317 G318 G319 Q320 E322 I331 R386 R388 G389
BS02
peptide
B
H108 Q111 H112 A140 F141 T142 E189 A198 W199 F202 K308 Y314 K364 E365 Q677 Q680
H65 Q68 H69 A97 F98 T99 E146 A155 W156 F159 K265 Y271 K321 E322 Q634 Q637
BS03
ZN
B
H108 H112 E189
H65 H69 E146
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
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:2wby
,
PDBe:2wby
,
PDBj:2wby
PDBsum
2wby
PubMed
19321446
UniProt
P14735
|IDE_HUMAN Insulin-degrading enzyme (Gene Name=IDE)
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