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Open data
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Basic information
| Entry | Database: PDB / ID: 9el1 | |||||||||||||||||||||
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| Title | ML2-SA1/PI(3,5)P2 bound TRPML2 in an open state | |||||||||||||||||||||
Components | Mucolipin-2 | |||||||||||||||||||||
Keywords | MEMBRANE PROTEIN / TRPML / calcium channel / ion transport | |||||||||||||||||||||
| Function / homology | Function and homology informationpositive regulation of macrophage inflammatory protein 1 alpha production / macrophage migration / NAADP-sensitive calcium-release channel activity / positive regulation of chemokine (C-C motif) ligand 5 production / iron ion transmembrane transporter activity / neutrophil migration / positive regulation of monocyte chemotactic protein-1 production / positive regulation of chemokine (C-X-C motif) ligand 2 production / TRP channels / calcium ion transmembrane transport ...positive regulation of macrophage inflammatory protein 1 alpha production / macrophage migration / NAADP-sensitive calcium-release channel activity / positive regulation of chemokine (C-C motif) ligand 5 production / iron ion transmembrane transporter activity / neutrophil migration / positive regulation of monocyte chemotactic protein-1 production / positive regulation of chemokine (C-X-C motif) ligand 2 production / TRP channels / calcium ion transmembrane transport / calcium channel activity / recycling endosome membrane / late endosome membrane / protein transport / adaptive immune response / lysosome / innate immune response / identical protein binding / membrane / plasma membrane Similarity search - Function | |||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.61 Å | |||||||||||||||||||||
Authors | Schmiege, P. / Li, X. | |||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: ML2-SA1/PI(3,5)P2 bound TRPML2 in an open state Authors: Schmiege, P. / Li, X. | |||||||||||||||||||||
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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 | 9el1.cif.gz | 382.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9el1.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9el1.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9el1_validation.pdf.gz | 2 MB | Display | wwPDB validaton report |
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| Full document | 9el1_full_validation.pdf.gz | 2.1 MB | Display | |
| Data in XML | 9el1_validation.xml.gz | 63.6 KB | Display | |
| Data in CIF | 9el1_validation.cif.gz | 91.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/el/9el1 ftp://data.pdbj.org/pub/pdb/validation_reports/el/9el1 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 48144MC 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: 66016.297 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MCOLN2 / Production host: Homo sapiens (human) / References: UniProt: Q8IZK6#2: Chemical | ChemComp-A1BI6 / ( Mass: 282.165 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C14H13Cl2NO / Feature type: SUBJECT OF INVESTIGATION #3: Chemical | ChemComp-EUJ / ( Has ligand of interest | Y | Has protein modification | Y | |
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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: ML2-SA1/PI(3,5)P2 bound TRPML2 / 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: 7.5 |
| Specimen | 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| CTF correction | Type: NONE |
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| 3D reconstruction | Resolution: 2.61 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 108226 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
United States, 1items
Citation
PDBj


FIELD EMISSION GUN