Structure of PDB 2wby Chain A
Receptor sequence
>2wbyA (length=957) Species:
9606
(Homo sapiens) [
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MNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALD
VHIGSLSDPPNIAGLSHFLQHMLFLGTKKYPKENEYSQFLSEHAGSSNAF
TSGEHTNYYFDVSHEHLEGALDRFAQFFLSPLFDESAKDREVNAVDSEHE
KNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQEL
LKFHSAYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEH
PFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHE
GPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDII
LHMFQYIQKLRAEGPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGIL
HYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDR
TEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLE
KEATPYPALIKDTAMSKLWFKQDDKFFLPKANLNFEFFSPFAYVDPLHSN
MAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPIL
LKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMT
EVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGI
MQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNSGI
EIYYQTDMQSTSENMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRAN
GIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAI
RRLDKPKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYK
EMLAVDAPRRHKVSVHVLAREMDSNLSQAPALPQPEVIQNMTEFKRGLPL
FPLVKPH
3D structure
PDB
2wby
Molecular Basis of Catalytic Chamber-Assisted Unfolding and Cleavage of Human Insulin by Human Insulin Degrading Enzyme.
Chain
A
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)
Q70
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
F141 Y150 H336 G339 E341 V360 G361 G362 Q363 E365 R429 R431 G432
F100 Y109 H295 G298 E300 V319 G320 G321 Q322 E324 R388 R390 G391
BS02
peptide
A
H108 Q111 H112 F141 E189 A198 W199 F202 K308 Y314 K364 E365
H67 Q70 H71 F100 E148 A157 W158 F161 K267 Y273 K323 E324
BS03
ZN
A
H108 H112 E189
H67 H71 E148
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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