Structure of PDB 2g56 Chain A Binding Site BS01
Receptor Information
>2g56 Chain A (length=964) Species:
9606
(Homo sapiens) [
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PAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHI
GSLSDPPNIAGLSHFCQHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSG
EHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNV
MNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKF
HSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQ
EEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPG
SLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHM
FQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYY
PLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEE
WYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEA
TPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAY
LYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKK
IIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVA
WTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQM
VEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIY
YQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQ
GLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRL
DKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEML
AVDAPRRHKVSVHVLAREMDSCPVVGNLSQAPALPQPEVIQNMTEFKRGL
PLFPLVKPHINFMA
Ligand information
>2g56 Chain C (length=18) Species:
9606
(Homo sapiens) [
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FVNQVEALYLVCGERGFF
Receptor-Ligand Complex Structure
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PDB
2g56
Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
H108 Q111 N139 A140 F141 T142 E189 W199 G339 E341 L359 V360 G361 Q680 M683 R824 Y831 R847
Binding residue
(residue number reindexed from 1)
H64 Q67 N95 A96 F97 T98 E145 W155 G295 E297 L315 V316 G317 Q636 M639 R780 Y787 R803
Enzymatic activity
Catalytic site (original residue number in PDB)
Q111
Catalytic site (residue number reindexed from 1)
Q67
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
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Cellular Component
External links
PDB
RCSB:2g56
,
PDBe:2g56
,
PDBj:2g56
PDBsum
2g56
PubMed
17051221
UniProt
P14735
|IDE_HUMAN Insulin-degrading enzyme (Gene Name=IDE)
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