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- EMDB-24757: Insulin Degrading Enzyme pO/pC -

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Basic information

Entry
Database: EMDB / ID: EMD-24757
TitleInsulin Degrading Enzyme pO/pC
Map dataInsulin Degrading Enzyme pO/pC
Sample
  • Complex: Cysteine-free Insulin-degrading enzyme in complex with Insulin A chain and Insulin B chain
    • Complex: Cysteine-free Insulin-degrading enzyme
      • Protein or peptide: Cysteine-free Insulin-degrading enzyme
    • Complex: Insulin A chain, Insulin B chain
      • Protein or peptide: Insulin A chain
      • Protein or peptide: Insulin B chain
KeywordsM16A zinc metalloprotease / HYDROLASE
Function / homology
Function and homology information


insulysin / beta-endorphin binding / ubiquitin recycling / insulin catabolic process / insulin metabolic process / amyloid-beta clearance by cellular catabolic process / hormone catabolic process / bradykinin catabolic process / cytosolic proteasome complex / insulin binding ...insulysin / beta-endorphin binding / ubiquitin recycling / insulin catabolic process / insulin metabolic process / amyloid-beta clearance by cellular catabolic process / hormone catabolic process / bradykinin catabolic process / cytosolic proteasome complex / insulin binding / regulation of aerobic respiration / negative regulation of glycogen catabolic process / positive regulation of nitric oxide mediated signal transduction / negative regulation of feeding behavior / negative regulation of fatty acid metabolic process / Signaling by Insulin receptor / peptide catabolic process / IRS activation / Insulin processing / regulation of protein secretion / positive regulation of peptide hormone secretion / positive regulation of respiratory burst / amyloid-beta clearance / Regulation of gene expression in beta cells / negative regulation of acute inflammatory response / peroxisomal matrix / alpha-beta T cell activation / positive regulation of dendritic spine maintenance / Synthesis, secretion, and deacylation of Ghrelin / negative regulation of respiratory burst involved in inflammatory response / amyloid-beta metabolic process / negative regulation of protein secretion / activation of protein kinase B activity / negative regulation of gluconeogenesis / positive regulation of insulin receptor signaling pathway / positive regulation of glycogen biosynthetic process / fatty acid homeostasis / Signal attenuation / positive regulation of protein binding / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / negative regulation of lipid catabolic process / positive regulation of lipid biosynthetic process / regulation of protein localization to plasma membrane / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / transport vesicle / nitric oxide-cGMP-mediated signaling / COPI-mediated anterograde transport / positive regulation of nitric-oxide synthase activity / Insulin receptor recycling / negative regulation of reactive oxygen species biosynthetic process / insulin-like growth factor receptor binding / positive regulation of brown fat cell differentiation / NPAS4 regulates expression of target genes / negative regulation of proteolysis / endoplasmic reticulum-Golgi intermediate compartment membrane / neuron projection maintenance / peptide binding / positive regulation of mitotic nuclear division / Insulin receptor signalling cascade / proteolysis involved in protein catabolic process / Peroxisomal protein import / positive regulation of glycolytic process / positive regulation of cytokine production / positive regulation of long-term synaptic potentiation / endosome lumen / acute-phase response / positive regulation of protein secretion / positive regulation of D-glucose import / insulin receptor binding / positive regulation of cell differentiation / Regulation of insulin secretion / wound healing / protein catabolic process / negative regulation of protein catabolic process / antigen processing and presentation of endogenous peptide antigen via MHC class I / hormone activity / positive regulation of neuron projection development / regulation of synaptic plasticity / metalloendopeptidase activity / positive regulation of protein localization to nucleus / Golgi lumen / cognition / glucose metabolic process / positive regulation of protein catabolic process / vasodilation / peroxisome / insulin receptor signaling pathway / glucose homeostasis / cell-cell signaling / regulation of protein localization / amyloid-beta binding / virus receptor activity / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of cell growth / protease binding / secretory granule lumen / endopeptidase activity / basolateral plasma membrane / positive regulation of canonical NF-kappaB signal transduction / Ub-specific processing proteases
Similarity search - Function
Peptidase M16, middle/third domain / Middle or third domain of peptidase_M16 / : / PQQ synthase PqqF-like, C-terminal lobe domain 4 / : / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal ...Peptidase M16, middle/third domain / Middle or third domain of peptidase_M16 / : / PQQ synthase PqqF-like, C-terminal lobe domain 4 / : / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / Insulin / Insulin family / Insulin-like / Insulin/IGF/Relaxin family / Insulin / insulin-like growth factor / relaxin family. / Insulin, conserved site / Insulin family signature. / Insulin-like superfamily
Similarity search - Domain/homology
Insulin / Insulin-degrading enzyme
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsMancl JM / Liang WG
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: To be published
Title: Ensemble cryoEM reveals a substrate-induced shift in the conformational dynamics of human insulin degrading enzyme
Authors: Mancl JM / Liang WG / Wei H / Carragher B / Potter CS / Tang WJ
History
DepositionAug 27, 2021-
Header (metadata) releaseAug 31, 2022-
Map releaseAug 31, 2022-
UpdateMay 28, 2025-
Current statusMay 28, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_24757.png

Downloads & links

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Map

FileDownload / File: emd_24757.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationInsulin Degrading Enzyme pO/pC
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 256 pix.
= 277.555 Å		1.08 Å/pix.
x 256 pix.
= 277.555 Å		1.08 Å/pix.
x 256 pix.
= 277.555 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.0842 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.03
Minimum - Maximum-0.12028788 - 0.22222795
Average (Standard dev.)-0.000012501205 (±0.006741864)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 277.5552 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Cysteine-free Insulin-degrading enzyme in complex with Insulin A ...

EntireName: Cysteine-free Insulin-degrading enzyme in complex with Insulin A chain and Insulin B chain
Components
  • Complex: Cysteine-free Insulin-degrading enzyme in complex with Insulin A chain and Insulin B chain
    • Complex: Cysteine-free Insulin-degrading enzyme
      • Protein or peptide: Cysteine-free Insulin-degrading enzyme
    • Complex: Insulin A chain, Insulin B chain
      • Protein or peptide: Insulin A chain
      • Protein or peptide: Insulin B chain

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Supramolecule #1: Cysteine-free Insulin-degrading enzyme in complex with Insulin A ...

SupramoleculeName: Cysteine-free Insulin-degrading enzyme in complex with Insulin A chain and Insulin B chain
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all

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Supramolecule #2: Cysteine-free Insulin-degrading enzyme

SupramoleculeName: Cysteine-free Insulin-degrading enzyme / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: Insulin A chain, Insulin B chain

SupramoleculeName: Insulin A chain, Insulin B chain / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2-#3
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Cysteine-free Insulin-degrading enzyme

MacromoleculeName: Cysteine-free Insulin-degrading enzyme / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: insulysin
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 117.068508 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MRYRLAWLLH PALPSTFRSV LGARLPPPER LCGFQKKTYS KMNNPAIKRI GNHITKSPED KREYRGLELA NGIKVLLISD PTTDKSSAA LDVHIGSLSD PPNIAGLSHF LEHMLFLGTK KYPKENEYSQ FLSEHAGSSN AFTSGEHTNY YFDVSHEHLE G ALDRFAQF ...String:
MRYRLAWLLH PALPSTFRSV LGARLPPPER LCGFQKKTYS KMNNPAIKRI GNHITKSPED KREYRGLELA NGIKVLLISD PTTDKSSAA LDVHIGSLSD PPNIAGLSHF LEHMLFLGTK KYPKENEYSQ FLSEHAGSSN AFTSGEHTNY YFDVSHEHLE G ALDRFAQF FLSPLFDESA KDREVNAVDS EHEKNVMNDA WRLFQLEKAT GNPKHPFSKF GTGNKYTLET RPNQEGIDVR QE LLKFHSA YYSSNLMAVV VLGRESLDDL TNLVVKLFSE VENKNVPLPE FPEHPFQEEH LKQLYKIVPI KDIRNLYVTF PIP DLQKYY KSNPGHYLGH LIGHEGPGSL LSELKSKGWV NTLVGGQKEG ARGFMFFIIN VDLTEEGLLH VEDIILHMFQ YIQK LRAEG PQEWVFQELK DLNAVAFRFK DKERPRGYTS KIAGILHYYP LEEVLTAEYL LEEFRPDLIE MVLDKLRPEN VRVAI VSKS FEGKTDRTEE WYGTQYKQEA IPDEVIKKWQ NADLNGKFKL PTKNEFIPTN FEILPLEKEA TPYPALIKDT AMSKLW FKQ DDKFFLPKAN LNFEFFSPFA YVDPLHSNMA YLYLELLKDS LNEYAYAAEL AGLSYDLQNT IYGMYLSVKG YNDKQPI LL KKIIEKMATF EIDEKRFEII KEAYMRSLNN FRAEQPHQHA MYYLRLLMTE VAWTKDELKE ALDDVTLPRL KAFIPQLL S RLHIEALLHG NITKQAALGI MQMVEDTLIE HAHTKPLLPS QLVRYREVQL PDRGWFVYQQ RNEVHNNSGI EIYYQTDMQ STSENMFLEL FAQIISEPAF NTLRTKEQLG YIVFSGPRRA NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKSIEDMTEE AFQKHIQAL AIRRLDKPKK LSAESAKYWG EIISQQYNFD RDNTEVAYLK TLTKEDIIKF YKEMLAVDAP RRHKVSVHVL A REMDSSPV VGEFPSQNDI NLSQAPALPQ PEVIQNMTEF KRGLPLFPLV KPH

UniProtKB: Insulin-degrading enzyme

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Macromolecule #2: Insulin A chain

MacromoleculeName: Insulin A chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 2.383698 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
GIVEQCCTSI CSLYQLENYC N

UniProtKB: Insulin

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Macromolecule #3: Insulin B chain

MacromoleculeName: Insulin B chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 3.417931 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
SequenceString:
FVNQHLCGSH LVEALYLVCG ERGFFYTPLT

UniProtKB: Insulin

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.2
VitrificationCryogen name: ETHANE / Instrument: SPOTITON

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 76379
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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