Structure of PDB 2wc0 Chain A
Receptor sequence
>2wc0A (length=952) Species:
9606
(Homo sapiens) [
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NNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDV
HIGSLSDPPNIAGLSHFLQHMLFLGTKKYPKENEYSQFLSEHAGSSNAFT
SGEHTNYYFDVSHEHLEGALDRFAQFFLSPLFDESAKDREVNAVDSEHEK
NVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELL
KFHSAYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHP
FQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEG
PGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIIL
HMFQYIQKLRAEGPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILH
YYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRT
EEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEK
EATPYPALIKDTAMSKLWFKQDDKFFLPKANLNFEFFSPFAYVDPLHSNM
AYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILL
KKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHHAMYYLRLLMTEV
AWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQ
MVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNSGIEI
YYQTDMQSTSENMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGI
QGLRFIIQSEKPPYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRL
DKPKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEML
AVDAPRRHKVSVHVLAREMNLSQAPALPQPEVIQNMTEFKRGLPLFPLVK
PH
3D structure
PDB
2wc0
Molecular Basis of Catalytic Chamber-Assisted Unfolding and Cleavage of Human Insulin by Human Insulin Degrading Enzyme.
Chain
A
Resolution
2.8 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)
Q69
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 S143 H336 G339 E341 L359 V360 G361 G362 Q363 E365 R429 R431 G432
F99 S101 H294 G297 E299 L317 V318 G319 G320 Q321 E323 R387 R389 G390
BS02
peptide
A
F141 T142 E189 A198 W199 F202 T220 Y314 E365 Q677
F99 T100 E147 A156 W157 F160 T178 Y272 E323 Q635
BS03
ZN
A
H108 H112 E189
H66 H70 E147
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:2wc0
,
PDBe:2wc0
,
PDBj:2wc0
PDBsum
2wc0
PubMed
19321446
UniProt
P14735
|IDE_HUMAN Insulin-degrading enzyme (Gene Name=IDE)
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