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Open data
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Basic information
| Entry | Database: PDB / ID: 8e6u | |||||||||||||||||||||
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| Title | Human TRPM2 ion channel in 1 mM F-dADPR | |||||||||||||||||||||
Components | Transient receptor potential cation channel subfamily M member 2 | |||||||||||||||||||||
Keywords | MEMBRANE PROTEIN / TRPM2 / TRP / ADPR / ADP-ribose / NUDT9H / NUDT9 / calcium / ion channel | |||||||||||||||||||||
| Function / homology | Function and homology informationmono-ADP-D-ribose binding / manganese ion transmembrane transporter activity / ligand-gated calcium channel activity / dendritic cell differentiation / zinc ion transmembrane transport / response to purine-containing compound / cellular response to temperature stimulus / regulation of filopodium assembly / response to hydroperoxide / dendritic cell chemotaxis ...mono-ADP-D-ribose binding / manganese ion transmembrane transporter activity / ligand-gated calcium channel activity / dendritic cell differentiation / zinc ion transmembrane transport / response to purine-containing compound / cellular response to temperature stimulus / regulation of filopodium assembly / response to hydroperoxide / dendritic cell chemotaxis / TRP channels / calcium ion transmembrane import into cytosol / temperature homeostasis / sodium channel activity / intracellularly gated calcium channel activity / calcium ion import across plasma membrane / tertiary granule membrane / ficolin-1-rich granule membrane / monoatomic cation channel activity / specific granule membrane / release of sequestered calcium ion into cytosol / cellular response to calcium ion / cytoplasmic vesicle membrane / cell projection / regulation of actin cytoskeleton organization / calcium ion transmembrane transport / calcium channel activity / cellular response to hydrogen peroxide / calcium ion transport / response to heat / perikaryon / protein homotetramerization / lysosome / lysosomal membrane / calcium ion binding / Neutrophil degranulation / plasma membrane Similarity search - Function | |||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||||||||||||||
Authors | Wang, L. / Fu, T.M. / Xia, S. / Wu, H. | |||||||||||||||||||||
| Funding support | 1items
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Citation | Journal: To Be PublishedTitle: A unified mechanism for human TRPM2 activation, desensitization and inhibition Authors: Wang, L. / Fu, T.-M. | |||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8e6u.cif.gz | 940.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8e6u.ent.gz | 775.9 KB | Display | PDB format |
| PDBx/mmJSON format | 8e6u.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8e6u_validation.pdf.gz | 2.1 MB | Display | wwPDB validaton report |
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| Full document | 8e6u_full_validation.pdf.gz | 2.2 MB | Display | |
| Data in XML | 8e6u_validation.xml.gz | 155.1 KB | Display | |
| Data in CIF | 8e6u_validation.cif.gz | 229.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e6/8e6u ftp://data.pdbj.org/pub/pdb/validation_reports/e6/8e6u | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 27926MC ![]() 8e6qC ![]() 8e6rC ![]() 8e6sC ![]() 8e6tC ![]() 8e6vC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 171416.188 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TRPM2, EREG1, KNP3, LTRPC2, TRPC7 / Production host: Homo sapiens (human) / References: UniProt: O94759#2: Chemical | ChemComp-UOZ / [( Mass: 619.412 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C21H27N5O13P2 / Feature type: SUBJECT OF INVESTIGATION Has ligand of interest | Y | Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Human TRPM2 in 1 mM F-dADPR / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.4 |
| Specimen | Conc.: 0.75 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 49 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.19_4092: / Classification: refinement | ||||||||||||||||||||||||
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| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 61503 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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Homo sapiens (human)
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