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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | TRPC5 in complex with spin-labelled ligand SpinPico1 | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Membrane protein / ion channel / inhibitor / non-covalent spin label / PROTEIN TRANSPORT | |||||||||
| Function / homology | Function and homology informationregulation of membrane hyperpolarization / phosphatidylserine exposure on apoptotic cell surface / negative regulation of dendrite morphogenesis / Role of second messengers in netrin-1 signaling / store-operated calcium channel activity / inositol 1,4,5 trisphosphate binding / cation channel complex / actinin binding / TRP channels / clathrin binding ...regulation of membrane hyperpolarization / phosphatidylserine exposure on apoptotic cell surface / negative regulation of dendrite morphogenesis / Role of second messengers in netrin-1 signaling / store-operated calcium channel activity / inositol 1,4,5 trisphosphate binding / cation channel complex / actinin binding / TRP channels / clathrin binding / regulation of cytosolic calcium ion concentration / positive regulation of axon extension / calcium channel complex / positive regulation of neuron differentiation / calcium ion transmembrane transport / calcium channel activity / neuron differentiation / calcium ion transport / nervous system development / presynapse / actin binding / positive regulation of cytosolic calcium ion concentration / growth cone / ATPase binding / neuron apoptotic process / neuronal cell body / positive regulation of cell population proliferation / dendrite / plasma membrane Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.32 Å | |||||||||
Authors | Porav SA / Bon RS | |||||||||
| Funding support | United Kingdom, 1 items
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Citation | Journal: To Be PublishedTitle: Non-covalent spin labelling of TRPC5 ion channels enables EPR studies of protein-ligand interactions Authors: Johnson AJ / Porav SA / Hammond KLR / Shah A / Hassane EM / Pask CM / Muench SP / Wilson AJ / Pilotas C / Bon RS | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_51416.map.gz | 323.7 MB | EMDB map data format | |
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| Header (meta data) | emd-51416-v30.xml emd-51416.xml | 23.5 KB 23.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_51416_fsc.xml | 14.7 KB | Display | FSC data file |
| Images | emd_51416.png | 119.8 KB | ||
| Masks | emd_51416_msk_1.map | 343 MB | Mask map | |
| Filedesc metadata | emd-51416.cif.gz | 6.9 KB | ||
| Others | emd_51416_additional_1.map.gz emd_51416_half_map_1.map.gz emd_51416_half_map_2.map.gz | 40 MB 318.2 MB 318.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51416 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51416 | HTTPS FTP |
-Validation report
| Summary document | emd_51416_validation.pdf.gz | 982.6 KB | Display | EMDB validaton report |
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| Full document | emd_51416_full_validation.pdf.gz | 982.2 KB | Display | |
| Data in XML | emd_51416_validation.xml.gz | 23 KB | Display | |
| Data in CIF | emd_51416_validation.cif.gz | 29.8 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51416 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51416 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9gkbMC ![]() 9gl6C 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_51416.map.gz / Format: CCP4 / Size: 343 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: 0.74 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_51416_msk_1.map | ||||||||||||
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| Density Histograms |
-Additional map: Resolve Cryo EM map
| File | emd_51416_additional_1.map | ||||||||||||
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| Annotation | Resolve_Cryo_EM map | ||||||||||||
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-Half map: #2
| File | emd_51416_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_51416_half_map_2.map | ||||||||||||
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Sample components
-Entire : TRPC5 homotetramer
| Entire | Name: TRPC5 homotetramer |
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| Components |
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-Supramolecule #1: TRPC5 homotetramer
| Supramolecule | Name: TRPC5 homotetramer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 480 KDa |
-Macromolecule #1: Short transient receptor potential channel 5
| Macromolecule | Name: Short transient receptor potential channel 5 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 89.00982 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MAQLYYKKVN YSPYRDRIPL QIVRAETELS AEEKAFLNAV EKGDYATVKQ ALQEAEIYYN VNINCMDPLG RSALLIAIEN ENLEIMELL LNHSVYVGDA LLYAIRKEVV GAVELLLSYR RPSGEKQVPT LMMDTQFSEF TPDITPIMLA AHTNNYEIIK L LVQKRVTI ...String: MAQLYYKKVN YSPYRDRIPL QIVRAETELS AEEKAFLNAV EKGDYATVKQ ALQEAEIYYN VNINCMDPLG RSALLIAIEN ENLEIMELL LNHSVYVGDA LLYAIRKEVV GAVELLLSYR RPSGEKQVPT LMMDTQFSEF TPDITPIMLA AHTNNYEIIK L LVQKRVTI PRPHQIRCNC VECVSSSEVD SLRHSRSRLN IYKALASPSL IALSSEDPIL TAFRLGWELK ELSKVENEFK AE YEELSQQ CKLFAKDLLD QARSSRELEI ILNHRDDHSE ELDPQKYHDL AKLKVAIKYH QKEFVAQPNC QQLLATLWYD GFP GWRRKH WVVKLLTCMT IGFLFPMLSI AYLISPRSNL GLFIKKPFIK FICHTASYLT FLFMLLLASQ HIVRTDLHVQ GPPP TVVEW MILPWVLGFI WGEIKEMWDG GFTEYIHDWW NLMDFAMNSL YLATISLKIM AYVKYNGSRP REEWEMWHPT LIAEA LFAI SNILSSLRLI SLFTANSHLG PLQISLGRML LDILKFLFIY CLVLLAFANG LNQLYFYYET RAIDEPNNCK GIRCEK QNN AFSTLFETLQ SLFWSVFGLL NLYVTNVKAR HEFTEFVGAT MFGTYNVISL VVLLNMLIAM MNNSYQLIAD HADIEWK FA RTKLWMSYFD EGGTLPPPFN IIPSPKSFLY LGNWFNNTFC PKRDPDGRRR RRNLRSFTER NADSLIQNQH YQEVIRNL V KRYVAAMIRN SKTHEGLTEE NFKELKQDIS SFRYEVLDLL GNRK UniProtKB: Short transient receptor potential channel 5 |
-Macromolecule #2: 7-[(4-chlorophenyl)methyl]-3-methyl-1-(3-oxidanylpropyl)-8-(2,2,6...
| Macromolecule | Name: 7-[(4-chlorophenyl)methyl]-3-methyl-1-(3-oxidanylpropyl)-8-(2,2,6,6-tetramethyl-1-oxidanyl-piperidin-4-yl)oxy-purine-2,6-dione type: ligand / ID: 2 / Number of copies: 4 / Formula: A1IMO |
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| Molecular weight | Theoretical: 520.021 Da |
-Macromolecule #3: CALCIUM ION
| Macromolecule | Name: CALCIUM ION / type: ligand / ID: 3 / Number of copies: 4 / Formula: CA |
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| Molecular weight | Theoretical: 40.078 Da |
-Macromolecule #4: CHOLESTEROL HEMISUCCINATE
| Macromolecule | Name: CHOLESTEROL HEMISUCCINATE / type: ligand / ID: 4 / Number of copies: 4 / Formula: Y01 |
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| Molecular weight | Theoretical: 486.726 Da |
| Chemical component information | ![]() ChemComp-Y01: |
-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 | 0.9 mg/mL | |||||||||
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| Buffer | pH: 7.4 Component:
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| Grid | Model: UltrAuFoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GOLD / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE | |||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Software | Name: EPU |
| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 35.5 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 30.0 µm / Nominal defocus min: 7.0 µm |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: Other / Chain - Initial model type: in silico model / Details: ModelAngelo |
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| Software | Name: Coot |
| Refinement | Protocol: AB INITIO MODEL |
| Output model | ![]() PDB-9gkb: |
Movie
Controller
About Yorodumi




Keywords
Homo sapiens (human)
Authors
United Kingdom, 1 items
Citation




Z (Sec.)
Y (Row.)
X (Col.)





















































FIELD EMISSION GUN

