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Yorodumi- PDB-10gh: Cryo-EM structure of Receptor Tyrosine Kinase ROS1 in complex wit... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 10gh | ||||||||||||||||||||||||
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| Title | Cryo-EM structure of Receptor Tyrosine Kinase ROS1 in complex with Fab-RX5 | ||||||||||||||||||||||||
Components |
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Keywords | TRANSFERASE/IMMUNE SYSTEM / Receptor tyrosine kinase / ROS1 extracellular bent-over conformation / Inhibitory Fab-RX5 / TRANSFERASE-IMMUNE SYSTEM complex | ||||||||||||||||||||||||
| Function / homology | Function and homology informationcolumnar/cuboidal epithelial cell development / regulation of phosphate transport / regulation of TOR signaling / regulation of ERK1 and ERK2 cascade / transmembrane receptor protein tyrosine kinase activity / cell surface receptor protein tyrosine kinase signaling pathway / regulation of cell growth / receptor protein-tyrosine kinase / protein tyrosine kinase activity / gene expression ...columnar/cuboidal epithelial cell development / regulation of phosphate transport / regulation of TOR signaling / regulation of ERK1 and ERK2 cascade / transmembrane receptor protein tyrosine kinase activity / cell surface receptor protein tyrosine kinase signaling pathway / regulation of cell growth / receptor protein-tyrosine kinase / protein tyrosine kinase activity / gene expression / protein phosphatase binding / spermatogenesis / cell differentiation / protein phosphorylation / receptor complex / negative regulation of gene expression / perinuclear region of cytoplasm / cell surface / signal transduction / ATP binding / plasma membrane Similarity search - Function | ||||||||||||||||||||||||
| Biological species | ![]() Homo sapiens (human) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.06 Å | ||||||||||||||||||||||||
Authors | Li, H. / Klein, D. | ||||||||||||||||||||||||
| Funding support | 1items
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Citation | Journal: To Be PublishedTitle: Clustering and a conformational switch drive activation of the mammalian receptor tyrosine kinase ROS1 Authors: Li, H. / Klein, D. | ||||||||||||||||||||||||
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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 | 10gh.cif.gz | 372 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb10gh.ent.gz | 238.1 KB | Display | PDB format |
| PDBx/mmJSON format | 10gh.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/0g/10gh ftp://data.pdbj.org/pub/pdb/validation_reports/0g/10gh | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 45172 ![]() 75151MC ![]() 10ftC 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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| 1 |
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Components
| #1: Protein | Mass: 112553.805 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Homo sapiens (human)References: UniProt: Q78DX7, receptor protein-tyrosine kinase | ||||||
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| #2: Antibody | Mass: 25079.678 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: ![]() | ||||||
| #3: Antibody | Mass: 25503.346 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: ![]() | ||||||
| #4: Polysaccharide | Source method: isolated from a genetically manipulated source #5: Sugar | ChemComp-NAG / Has ligand of interest | N | Has protein modification | Y | |
-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: Receptor tyrosine kinase ROS1 in complex with Fab-RX5 / Type: COMPLEX / Entity ID: #1-#3 / Source: MULTIPLE SOURCES |
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| Source (natural) | Organism: ![]() |
| 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: 2000 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.06 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 166992 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
| Displacement parameters | Biso mean: 82.87 Å2 | ||||||||||||||||||||||||
| Refine LS restraints |
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Homo sapiens (human)
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