+Open data
-Basic information
Entry | Database: PDB / ID: 5hz1 | |||||||||
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Title | Plant peptide hormone receptor RGFR1 in complex with RGF3 | |||||||||
Components |
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Keywords | TRANSFERASE / Plant Receptor | |||||||||
Function / homology | Function and homology information maintenance of meristem identity / regulation of lateral root development / regulation of root morphogenesis / regulation of root development / maintenance of root meristem identity / regulation of root meristem growth / peptide receptor activity / regulation of asymmetric cell division / growth factor activity / peptide binding ...maintenance of meristem identity / regulation of lateral root development / regulation of root morphogenesis / regulation of root development / maintenance of root meristem identity / regulation of root meristem growth / peptide receptor activity / regulation of asymmetric cell division / growth factor activity / peptide binding / cell differentiation / non-specific serine/threonine protein kinase / protein serine kinase activity / protein serine/threonine kinase activity / positive regulation of cell population proliferation / positive regulation of gene expression / extracellular space / ATP binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Arabidopsis thaliana (thale cress) Arabidopsis (plant) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.59 Å | |||||||||
Authors | Song, W. / Han, Z. / Chai, J. | |||||||||
Citation | Journal: To Be Published Title: Plant Receptor Authors: Song, W. / Han, Z. / Chai, J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5hz1.cif.gz | 132.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5hz1.ent.gz | 104.3 KB | Display | PDB format |
PDBx/mmJSON format | 5hz1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5hz1_validation.pdf.gz | 831.5 KB | Display | wwPDB validaton report |
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Full document | 5hz1_full_validation.pdf.gz | 839.2 KB | Display | |
Data in XML | 5hz1_validation.xml.gz | 23.1 KB | Display | |
Data in CIF | 5hz1_validation.cif.gz | 31.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hz/5hz1 ftp://data.pdbj.org/pub/pdb/validation_reports/hz/5hz1 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 69202.875 Da / Num. of mol.: 1 / Fragment: UNP residues 57-689 / Mutation: V64T, G81E, M82K, D83Q, N104Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: At4g26540, M3E9.30 Production host: Insect cell expression vector pTIE1 (others) References: UniProt: C0LGR3, non-specific serine/threonine protein kinase |
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#2: Protein/peptide | Mass: 1763.826 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Arabidopsis (plant) / References: UniProt: Q6ID76*PLUS |
#3: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
#4: Sugar |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 4 Å3/Da / Density % sol: 69.24 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 0.1 M MES monohydrate pH 6.0, 22% (v/v) polyethylene glycol (PEG) 400 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 1 Å |
Detector | Type: OXFORD RUBY CCD / Detector: CCD / Date: Dec 21, 2014 |
Radiation | Protocol: LAUE / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.59→99 Å / Num. obs: 33780 / % possible obs: 98.9 % / Redundancy: 5.2 % / Net I/σ(I): 31.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.59→35.42 Å / Cor.coef. Fo:Fc: 0.934 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.363 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||
Displacement parameters | Biso max: 214.61 Å2 / Biso mean: 25.686 Å2 / Biso min: 2 Å2
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Refinement step | Cycle: final / Resolution: 2.59→35.42 Å
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LS refinement shell | Resolution: 2.591→2.659 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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