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Open data
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Basic information
Entry | Database: PDB / ID: 5xjx | ||||||
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Title | Pre-formed plant receptor ERL1-TMM complex | ||||||
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![]() | TRANSFERASE/MEMBRANE PROTEIN / receptor like kinase / receptor like protein / pre-formed complexe / TRANSFERASE-MEMBRANE PROTEIN complex | ||||||
Function / homology | ![]() regulation of antifungal innate immune response / trichome morphogenesis / stomatal complex morphogenesis / stomatal complex formation / stomatal complex patterning / cellular response to abscisic acid stimulus / plant ovule development / embryo sac development / asymmetric cell division / response to abscisic acid ...regulation of antifungal innate immune response / trichome morphogenesis / stomatal complex morphogenesis / stomatal complex formation / stomatal complex patterning / cellular response to abscisic acid stimulus / plant ovule development / embryo sac development / asymmetric cell division / response to abscisic acid / receptor serine/threonine kinase binding / defense response to fungus / peptide binding / non-specific serine/threonine protein kinase / phosphorylation / innate immune response / protein serine kinase activity / signaling receptor binding / protein serine/threonine kinase activity / ATP binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Chai, J. / Lin, G. / Zhang, L. / Han, Z. / Yang, X. / Liu, W. / Qi, Y. / Chang, J. / Li, E. | ||||||
Funding support | ![]()
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![]() | ![]() Title: A receptor-like protein acts as a specificity switch for the regulation of stomatal development. Authors: Lin, G. / Zhang, L. / Han, Z. / Yang, X. / Liu, W. / Li, E. / Chang, J. / Qi, Y. / Shpak, E.D. / Chai, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.9 MB | Display | ![]() |
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PDB format | ![]() | 1.6 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 542.7 KB | Display | ![]() |
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Full document | ![]() | 607.8 KB | Display | |
Data in XML | ![]() | 172.6 KB | Display | |
Data in CIF | ![]() | 233.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5xjoC ![]() 5xkjC ![]() 5xknC ![]() 4mn8S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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6 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 47465.742 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 60516.891 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: C0LGW6, non-specific serine/threonine protein kinase |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.66 Å3/Da / Density % sol: 66.4 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 4% v/v Tacsimate pH 6.0, 10% w/v Polyethylene glycol 3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAC Science DIP-320 / Detector: IMAGE PLATE / Date: Oct 7, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 3.05→50 Å / Num. obs: 158048 / % possible obs: 98.5 % / Redundancy: 3 % / Net I/σ(I): 14 |
Reflection shell | Resolution: 3.0553→3.0901 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4MN8 Resolution: 3.055→43.249 Å / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 1.97 / Phase error: 30.3
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.055→43.249 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -50.2109 Å / Origin y: 67.4422 Å / Origin z: -126.1754 Å
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Refinement TLS group | Selection details: all |