+Open data
-Basic information
Entry | Database: PDB / ID: 5xjo | ||||||
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Title | Plant receptor ERL1-TMM in complex with peptide EPF1 | ||||||
Components |
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Keywords | TRANSFERASE/MEMBRANE PROTEIN / plant receptor / pre-formed complex / peptide hormone / TRANSFERASE-MEMBRANE PROTEIN complex | ||||||
Function / homology | Function and homology information negative regulation of stomatal complex development / regulation of antifungal innate immune response / guard cell differentiation / trichome morphogenesis / stomatal complex morphogenesis / stomatal complex formation / stomatal complex patterning / cellular response to abscisic acid stimulus / stomatal complex development / plant ovule development ...negative regulation of stomatal complex development / regulation of antifungal innate immune response / guard cell differentiation / trichome morphogenesis / stomatal complex morphogenesis / stomatal complex formation / stomatal complex patterning / cellular response to abscisic acid stimulus / stomatal complex development / 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 / signaling receptor binding / protein serine kinase activity / innate immune response / protein serine/threonine kinase activity / extracellular region / ATP binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.626 Å | ||||||
Authors | Chai, J. / Lin, G. / Zhang, L. / Han, Z. / Shpak, E.D. / Yang, X. | ||||||
Funding support | China, 1items
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Citation | Journal: Genes Dev. / Year: 2017 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5xjo.cif.gz | 680.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5xjo.ent.gz | 582 KB | Display | PDB format |
PDBx/mmJSON format | 5xjo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xj/5xjo ftp://data.pdbj.org/pub/pdb/validation_reports/xj/5xjo | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 58612.699 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: ERL1, At5g62230, MMI9.14 / Production host: Trichoplusia ni (cabbage looper) References: UniProt: C0LGW6, non-specific serine/threonine protein kinase #2: Protein | Mass: 5539.479 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: EPF1, At2g20875, F5H14 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q8S8I4 #3: Protein | Mass: 41410.285 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: TMM, RLP17, At1g80080, F18B13.16 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q9SSD1 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.78 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Ammonium citrate tribasic pH 7.0, polyethylene glycol 3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 14-BM-C / Wavelength: 0.979 Å |
Detector | Type: CS-PAD XPP / Detector: PIXEL / Date: Nov 1, 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: 2.626→50 Å / Num. obs: 65476 / % possible obs: 94.6 % / Redundancy: 3.2 % / Net I/σ(I): 16.3 |
Reflection shell | Resolution: 2.626→42.5395 Å |
-Processing
Software |
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Refinement | Resolution: 2.626→42.534 Å / SU ML: 0.4 / Cross valid method: FREE R-VALUE / σ(F): 1.98 / Phase error: 35.05 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.626→42.534 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: -28.8832 Å / Origin y: 20.6191 Å / Origin z: 26.4486 Å
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Refinement TLS group | Selection details: all |