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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Tetrameric 5-HT3A receptor in Salipro (holo, asymmetric) | |||||||||
Map data | unfiltered EM map | |||||||||
Sample |
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Keywords | 5-HT3R / Serotonin / receptor / tetramer / ion channel MEMBRANE PROTEIN / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationNeurotransmitter receptors and postsynaptic signal transmission / serotonin-gated cation-selective signaling pathway / serotonin-activated cation-selective channel complex / serotonin-gated monoatomic cation channel activity / serotonin receptor signaling pathway / serotonin binding / : / cleavage furrow / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / postsynaptic membrane / identical protein binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||
Authors | Introini B / Kudryashev M | |||||||||
| Funding support | Germany, 1 items
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Citation | Journal: Protein Sci / Year: 2018 Title: UCSF ChimeraX: Meeting modern challenges in visualization and analysis. Authors: Thomas D Goddard / Conrad C Huang / Elaine C Meng / Eric F Pettersen / Gregory S Couch / John H Morris / Thomas E Ferrin / ![]() Abstract: UCSF ChimeraX is next-generation software for the visualization and analysis of molecular structures, density maps, 3D microscopy, and associated data. It addresses challenges in the size, scope, and ...UCSF ChimeraX is next-generation software for the visualization and analysis of molecular structures, density maps, 3D microscopy, and associated data. It addresses challenges in the size, scope, and disparate types of data attendant with cutting-edge experimental methods, while providing advanced options for high-quality rendering (interactive ambient occlusion, reliable molecular surface calculations, etc.) and professional approaches to software design and distribution. This article highlights some specific advances in the areas of visualization and usability, performance, and extensibility. ChimeraX is free for noncommercial use and is available from http://www.rbvi.ucsf.edu/chimerax/ for Windows, Mac, and Linux. | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_16387.map.gz | 67.1 MB | EMDB map data format | |
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| Header (meta data) | emd-16387-v30.xml emd-16387.xml | 19 KB 19 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_16387_fsc.xml | 11.7 KB | Display | FSC data file |
| Images | emd_16387.png | 49.2 KB | ||
| Masks | emd_16387_msk_1.map | 137.1 MB | Mask map | |
| Filedesc metadata | emd-16387.cif.gz | 6 KB | ||
| Others | emd_16387_additional_1.map.gz emd_16387_half_map_1.map.gz emd_16387_half_map_2.map.gz | 129.3 MB 127.1 MB 127.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-16387 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-16387 | HTTPS FTP |
-Validation report
| Summary document | emd_16387_validation.pdf.gz | 783.4 KB | Display | EMDB validaton report |
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| Full document | emd_16387_full_validation.pdf.gz | 783 KB | Display | |
| Data in XML | emd_16387_validation.xml.gz | 19.3 KB | Display | |
| Data in CIF | emd_16387_validation.cif.gz | 25.5 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16387 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16387 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8c21MC ![]() 8c1wC ![]() 8c1zC ![]() 8c20C 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_16387.map.gz / Format: CCP4 / Size: 137.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | unfiltered EM map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.837 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_16387_msk_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Additional map: filtered EM map used for model generation and fitting
| File | emd_16387_additional_1.map | ||||||||||||
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| Annotation | filtered EM map used for model generation and fitting | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: unfiltered half map A
| File | emd_16387_half_map_1.map | ||||||||||||
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| Annotation | unfiltered half map A | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: unfiltered half map B
| File | emd_16387_half_map_2.map | ||||||||||||
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| Annotation | unfiltered half map B | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Tetrameric 5-HT3aR receptor in Salipro (holo, asymmetric)
| Entire | Name: Tetrameric 5-HT3aR receptor in Salipro (holo, asymmetric) |
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| Components |
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-Supramolecule #1: Tetrameric 5-HT3aR receptor in Salipro (holo, asymmetric)
| Supramolecule | Name: Tetrameric 5-HT3aR receptor in Salipro (holo, asymmetric) type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 220 KDa |
-Macromolecule #1: 5-hydroxytryptamine receptor 3A
| Macromolecule | Name: 5-hydroxytryptamine receptor 3A / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 60.668086 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MWSHPQFEKG GGSGGGSGGG SWSHPQFEKG GGSGGGSGGG SWSHPQFEKG GGSGGGSGGG SWSHPQFEKE NLYFQGATQA RDTTQPALL RLSDHLLANY KKGVRPVRDW RKPTTVSIDV IMYAILNVDE KNQVLTTYIW YRQYWTDEFL QWTPEDFDNV T KLSIPTDS ...String: MWSHPQFEKG GGSGGGSGGG SWSHPQFEKG GGSGGGSGGG SWSHPQFEKG GGSGGGSGGG SWSHPQFEKE NLYFQGATQA RDTTQPALL RLSDHLLANY KKGVRPVRDW RKPTTVSIDV IMYAILNVDE KNQVLTTYIW YRQYWTDEFL QWTPEDFDNV T KLSIPTDS IWVPDILINE FVDVGKSPNI PYVYVHHRGE VQNYKPLQLV TACSLDIYNF PFDVQNCSLT FTSWLHTIQD IN ITLWRSP EEVRSDKSIF INQGEWELLE VFPQFKEFSI DISNSYAEMK FYVIIRRRPL FYAVSLLLPS IFLMVVDIVG FCL PPDSGE RVSFKITLLL GYSVFLIIVS DTLPATAIGT PLIGVYFVVC MALLVISLAE TIFIVRLVHK QDLQRPVPDW LRHL VLDRI AWILCLGEQP MAHRPPATFQ ANKTDDCSGS DLLPAMGNHC SHVGGPQDLE KTPRGRGSPL PPPREASLAV RGLLQ ELSS IRHFLEKRDE MREVARDWLR VGYVLDRLLF RIYLLAVLAY SITLVTLWSI WHSS UniProtKB: 5-hydroxytryptamine receptor 3A |
-Macromolecule #2: SEROTONIN
| Macromolecule | Name: SEROTONIN / type: ligand / ID: 2 / Number of copies: 2 / Formula: SRO |
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| Molecular weight | Theoretical: 176.215 Da |
| Chemical component information | ![]() ChemComp-SRO: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.6 |
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| Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 55.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.3 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
Germany, 1 items
Citation











Z (Sec.)
Y (Row.)
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Homo sapiens (human)
Processing
FIELD EMISSION GUN


