Structure of PDB 2g48 Chain B
Receptor sequence
>2g48B (length=966) Species:
9606
(Homo sapiens) [
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NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVH
IGSLSDPPNIAGLSHFCQHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTS
GEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKN
VMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLK
FHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPF
QEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGP
GSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILH
MFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHY
YPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTE
EWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKE
ATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMA
YLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLK
KIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEV
AWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQ
MVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEI
YYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGI
QGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRR
LDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEM
LAVDAPRRHKVSVHVLAREMDSCPVVGEFINLSQAPALPQPEVIQNMTEF
KRGLPLFPLVKPHINF
3D structure
PDB
2g48
Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism.
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
H108 Q111 H112 F115 N139 A140 F141 T142 Y150 E189 K192 W199 F202 T220 G339 E341 L359 V360 G361 Q363 M683 R824 Y831 I832 F834 R847 I849
H65 Q68 H69 F72 N96 A97 F98 T99 Y107 E146 K149 W156 F159 T177 G296 E298 L316 V317 G318 Q320 M640 R781 Y788 I789 F791 R804 I806
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:2g48
,
PDBe:2g48
,
PDBj:2g48
PDBsum
2g48
PubMed
17051221
UniProt
P14735
|IDE_HUMAN Insulin-degrading enzyme (Gene Name=IDE)
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