+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-24759 | |||||||||
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Title | Insulin Degrading Enzyme O/pO | |||||||||
Map data | Insulin Degrading Enzyme O/pO | |||||||||
Sample |
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Keywords | M16A zinc metalloprotease / HYDROLASE | |||||||||
Function / homology | Function and homology information insulysin / ubiquitin recycling / insulin catabolic process / insulin metabolic process / amyloid-beta clearance by cellular catabolic process / hormone catabolic process / bradykinin catabolic process / insulin binding / regulation of aerobic respiration / peptide catabolic process ...insulysin / ubiquitin recycling / insulin catabolic process / insulin metabolic process / amyloid-beta clearance by cellular catabolic process / hormone catabolic process / bradykinin catabolic process / insulin binding / regulation of aerobic respiration / peptide catabolic process / amyloid-beta clearance / peroxisomal matrix / amyloid-beta metabolic process / Insulin receptor recycling / proteolysis involved in protein catabolic process / Peroxisomal protein import / peptide binding / protein catabolic process / antigen processing and presentation of endogenous peptide antigen via MHC class I / metalloendopeptidase activity / positive regulation of protein catabolic process / peroxisome / positive regulation of protein binding / insulin receptor signaling pathway / virus receptor activity / basolateral plasma membrane / endopeptidase activity / Ub-specific processing proteases / external side of plasma membrane / cell surface / protein homodimerization activity / mitochondrion / proteolysis / extracellular space / extracellular exosome / zinc ion binding / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.1 Å | |||||||||
Authors | Mancl JM / Liang WG | |||||||||
Funding support | United States, 1 items
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Citation | Journal: 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 |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_24759.map.gz | 59.9 MB | EMDB map data format | |
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Header (meta data) | emd-24759-v30.xml emd-24759.xml | 9.3 KB 9.3 KB | Display Display | EMDB header |
Images | emd_24759.png | 54.4 KB | ||
Filedesc metadata | emd-24759.cif.gz | 5.5 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-24759 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-24759 | HTTPS FTP |
-Validation report
Summary document | emd_24759_validation.pdf.gz | 624.9 KB | Display | EMDB validaton report |
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Full document | emd_24759_full_validation.pdf.gz | 624.4 KB | Display | |
Data in XML | emd_24759_validation.xml.gz | 6 KB | Display | |
Data in CIF | emd_24759_validation.cif.gz | 6.9 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-24759 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-24759 | HTTPS FTP |
-Related structure data
Related structure data | 7rzgMC 7rzeC 7rzfC 7rzhC 7rziC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_24759.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Insulin Degrading Enzyme O/pO | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.0842 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
-Entire : Cysteine-free Insulin-degrading enzyme
Entire | Name: Cysteine-free Insulin-degrading enzyme |
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Components |
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-Supramolecule #1: Cysteine-free Insulin-degrading enzyme
Supramolecule | Name: Cysteine-free Insulin-degrading enzyme / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Cysteine-free Insulin-degrading enzyme
Macromolecule | Name: Cysteine-free Insulin-degrading enzyme / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: insulysin |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 117.068508 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: 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 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.2 |
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Vitrification | Cryogen name: ETHANE / Instrument: SPOTITON |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: INSILICO MODEL |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 328870 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |