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- PDB-2mma: NMR-based docking model of GrxS14-BolA2 apo-heterodimer from Arab... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2mma | ||||||
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Title | NMR-based docking model of GrxS14-BolA2 apo-heterodimer from Arabidopsis thaliana | ||||||
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![]() | GENE REGULATION / stress-responsive protein / transcriptional regulator | ||||||
Function / homology | ![]() protein maturation by iron-sulfur cluster transfer / chloroplast envelope / antiporter activity / response to iron ion / chloroplast stroma / monoatomic cation transport / chloroplast / 2 iron, 2 sulfur cluster binding / intracellular iron ion homeostasis / response to oxidative stress ...protein maturation by iron-sulfur cluster transfer / chloroplast envelope / antiporter activity / response to iron ion / chloroplast stroma / monoatomic cation transport / chloroplast / 2 iron, 2 sulfur cluster binding / intracellular iron ion homeostasis / response to oxidative stress / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics, energy minimization | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Roret, T. / Tsan, P. / Couturier, J. / Rouhier, N. / Didierjean, C. | ||||||
![]() | ![]() Title: Structural and Spectroscopic Insights into BolA-Glutaredoxin Complexes. Authors: Roret, T. / Tsan, P. / Couturier, J. / Zhang, B. / Johnson, M.K. / Rouhier, N. / Didierjean, C. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 70.8 KB | Display | ![]() |
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PDB format | ![]() | 53.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.8 KB | Display | ![]() |
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Full document | ![]() | 440 KB | Display | |
Data in XML | ![]() | 7.7 KB | Display | |
Data in CIF | ![]() | 10.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2mm9C ![]() 4pugC ![]() 4puhC ![]() 4puiC 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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NMR ensembles |
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Components
#1: Protein | Mass: 12354.149 Da / Num. of mol.: 1 / Fragment: UNP residues 67-173 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 10258.644 Da / Num. of mol.: 1 / Fragment: UNP residues 2-81 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.05 / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: molecular dynamics, energy minimization / Software ordinal: 1 Details: Energy minimization using the YASARA force field. The structure was moved to a nearby (local) minimum, with removal of clashes and small errors. | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 1 / Conformers submitted total number: 1 |