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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Cryo-EM structure of human sortilin ectodomain | |||||||||
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Sample |
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Keywords | Trafficking / Vacuolar Protein Sorting / VPS10 / Beta propeller / Neurotensin binding receptor 3 / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationneurotensin receptor activity, non-G protein-coupled / Golgi to lysosome transport / plasma membrane to endosome transport / myotube differentiation / nerve growth factor receptor activity / cerebellar climbing fiber to Purkinje cell synapse / maintenance of synapse structure / retromer complex binding / Golgi to endosome transport / endosome transport via multivesicular body sorting pathway ...neurotensin receptor activity, non-G protein-coupled / Golgi to lysosome transport / plasma membrane to endosome transport / myotube differentiation / nerve growth factor receptor activity / cerebellar climbing fiber to Purkinje cell synapse / maintenance of synapse structure / retromer complex binding / Golgi to endosome transport / endosome transport via multivesicular body sorting pathway / vesicle organization / nerve growth factor binding / protein targeting to lysosome / trans-Golgi network transport vesicle / clathrin-coated vesicle / Golgi cisterna membrane / endosome to lysosome transport / Golgi Associated Vesicle Biogenesis / negative regulation of fat cell differentiation / neurotrophin TRK receptor signaling pathway / : / extrinsic apoptotic signaling pathway via death domain receptors / neuropeptide signaling pathway / clathrin-coated pit / ossification / response to insulin / endocytosis / regulation of gene expression / cytoplasmic vesicle / nuclear membrane / early endosome / lysosome / endosome membrane / G protein-coupled receptor signaling pathway / lysosomal membrane / endoplasmic reticulum membrane / perinuclear region of cytoplasm / enzyme binding / cell surface / Golgi apparatus / membrane / plasma membrane / cytosol Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
Authors | Boniardi I / Coscia F | |||||||||
| Funding support | European Union, 1 items
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Citation | Journal: To Be PublishedTitle: Cryo-EM structure of human sortilin ectodomain Authors: Boniardi I / Coscia F | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_52562.map.gz | 139.9 MB | EMDB map data format | |
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| Header (meta data) | emd-52562-v30.xml emd-52562.xml | 18.3 KB 18.3 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_52562_fsc.xml | 11.3 KB | Display | FSC data file |
| Images | emd_52562.png | 111.7 KB | ||
| Filedesc metadata | emd-52562.cif.gz | 6.7 KB | ||
| Others | emd_52562_half_map_1.map.gz emd_52562_half_map_2.map.gz | 137.8 MB 137.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-52562 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-52562 | HTTPS FTP |
-Validation report
| Summary document | emd_52562_validation.pdf.gz | 765.8 KB | Display | EMDB validaton report |
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| Full document | emd_52562_full_validation.pdf.gz | 765.3 KB | Display | |
| Data in XML | emd_52562_validation.xml.gz | 20.4 KB | Display | |
| Data in CIF | emd_52562_validation.cif.gz | 26.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-52562 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-52562 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9i0nMC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_52562.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.748 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_52562_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_52562_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Sortilin ectodomain
| Entire | Name: Sortilin ectodomain |
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| Components |
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-Supramolecule #1: Sortilin ectodomain
| Supramolecule | Name: Sortilin ectodomain / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 Details: Sortilin ectodomain, mature form generated by furin proteolysis of its N-terminal propeptide. The protein is recombinantly produced in mammalian cells and purified using a C-terminal poly-his tag |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Sortilin
| Macromolecule | Name: Sortilin / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 82.94057 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: QDRLDAPPPP AAPLPRWSGP IGVSWGLRAA AAGGAFPRGG RWRRSAPGED EECGRVRDFV AKLANNTHQH VFDDLRGSVS LSWVGDSTG VILVLTTFHV PLVIMTFGQS KLYRSEDYGK NFKDITDLIN NTFIRTEFGM AIGPENSGKV VLTAEVSGGS R GGRIFRSS ...String: QDRLDAPPPP AAPLPRWSGP IGVSWGLRAA AAGGAFPRGG RWRRSAPGED EECGRVRDFV AKLANNTHQH VFDDLRGSVS LSWVGDSTG VILVLTTFHV PLVIMTFGQS KLYRSEDYGK NFKDITDLIN NTFIRTEFGM AIGPENSGKV VLTAEVSGGS R GGRIFRSS DFAKNFVQTD LPFHPLTQMM YSPQNSDYLL ALSTENGLWV SKNFGGKWEE IHKAVCLAKW GSDNTIFFTT YA NGSCKAD LGALELWRTS DLGKSFKTIG VKIYSFGLGG RFLFASVMAD KDTTRRIHVS TDQGDTWSMA QLPSVGQEQF YSI LAANDD MVFMHVDEPG DTGFGTIFTS DDRGIVYSKS LDRHLYTTTG GETDFTNVTS LRGVYITSVL SEDNSIQTMI TFDQ GGRWT HLRKPENSEC DATAKNKNEC SLHIHASYSI SQKLNVPMAP LSEPNAVGIV IAHGSVGDAI SVMVPDVYIS DDGGY SWTK MLEGPHYYTI LDSGGIIVAI EHSSRPINVI KFSTDEGQCW QTYTFTRDPI YFTGLASEPG ARSMNISIWG FTESFL TSQ WVSYTIDFKD ILERNCEEKD YTIWLAHSTD PEDYEDGCIL GYKEQFLRLR KSSVCQNGRD YVVTKQPSIC LCSLEDF LC DFGYYRPEND SKCVEQPELK GHDLEFCLYG REEHLTTNGY RKIPGDKCQG GVNPVREVKD LKKKCTSNFL SPEKQNSK S NSENLYFQSA GHHHHHHHHH H UniProtKB: Sortilin |
-Macromolecule #3: 2-acetamido-2-deoxy-beta-D-glucopyranose
| Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 3 / Number of copies: 1 / Formula: NAG |
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| Molecular weight | Theoretical: 221.208 Da |
| Chemical component information | ![]() ChemComp-NAG: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 2.5 mg/mL | ||||||||||||
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| Buffer | pH: 7.5 Component:
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| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. | ||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Energy filter - Name: TFS Selectris X / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: TFS FALCON 4i (4k x 4k) / Number real images: 15781 / 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 / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
Citation

Z (Sec.)
Y (Row.)
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Processing
FIELD EMISSION GUN


