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Open data
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Basic information
Entry | Database: PDB / ID: 5gzz | ||||||
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Title | Crystal Structure of FIN219-SjGST complex with JA | ||||||
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![]() | LIGASE/TRANSFERASE / Jasmonate-amido synthetase / Glutathione S-transferase / Ligase-Transferase complex | ||||||
Function / homology | ![]() jasmonoyl-L-amino acid ligase / jasmonoyl-L-amino acid ligase activity / regulation of response to red or far red light / cellular response to auxin stimulus / induced systemic resistance, jasmonic acid mediated signaling pathway / L-leucine binding / acid-amino acid ligase activity / response to mycotoxin / protein adenylylation / response to UV-B ...jasmonoyl-L-amino acid ligase / jasmonoyl-L-amino acid ligase activity / regulation of response to red or far red light / cellular response to auxin stimulus / induced systemic resistance, jasmonic acid mediated signaling pathway / L-leucine binding / acid-amino acid ligase activity / response to mycotoxin / protein adenylylation / response to UV-B / amino acid binding / glutathione transferase / glutathione transferase activity / glutathione metabolic process / enzyme binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Chen, C.Y. / Cheng, Y.S. | ||||||
![]() | ![]() Title: Structural basis of jasmonate-amido synthetase FIN219 in complex with glutathione S-transferase FIP1 during the JA signal regulation Authors: Chen, C.Y. / Ho, S.S. / Kuo, T.Y. / Hsieh, H.L. / Cheng, Y.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 402 KB | Display | ![]() |
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PDB format | ![]() | 327.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5echC ![]() 5eciC ![]() 5eckC ![]() 5eclC ![]() 5ecmC ![]() 5ecnC ![]() 5ecoC ![]() 5ecpC ![]() 5ecqC ![]() 5ecrC ![]() 5ecsC ![]() 4eplS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Details | Chain D-G are the molecular packing in the protein crystal and not included in the unit of biological assembly |
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Components
#1: Protein | Mass: 64416.199 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9SKE2, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) | ||||||
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#2: Protein | Mass: 25534.723 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Chemical | ChemComp-JAA / {( | #4: Chemical | ChemComp-GSH / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.03 % / Mosaicity: 1.227 ° / Mosaicity esd: 0.012 ° |
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Crystal grow | Temperature: 297 K / Method: vapor diffusion / pH: 8.5 Details: 0.2 M Magnesium chloride hexahydrate, 0.1 M Tris-HCl, 40%(w/v) PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: RAYONIX MX-300 / Detector: CCD / Date: Mar 30, 2012 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: LAUE / Monochromatic (M) / Laue (L): L / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.4→50 Å / Num. obs: 73703 / % possible obs: 97.5 % / Redundancy: 1.9 % / Biso Wilson estimate: 13.22 Å2 / Rmerge(I) obs: 0.05 / Χ2: 1.006 / Net I/av σ(I): 15.426 / Net I/σ(I): 10.1 / Num. measured all: 141298 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: _
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4EPL Resolution: 2.386→26.209 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.45 / Phase error: 19.07 / 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 82.11 Å2 / Biso mean: 15.9573 Å2 / Biso min: 2 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.386→26.209 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30
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