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- PDB-2xn7: Crystal structure of thyroxine-binding globulin complexed with th... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2xn7 | |||||||||
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Title | Crystal structure of thyroxine-binding globulin complexed with thyroxine-fluoresein (T405-CF) | |||||||||
![]() | (THYROXINE-BINDING ...) x 2 | |||||||||
![]() | TRANSPORT / CLEAVED PROTEIN | |||||||||
Function / homology | ![]() thyroid hormone transport / serine-type endopeptidase inhibitor activity / extracellular space / extracellular exosome / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Qi, X. / Yan, Y. / Wei, Z. / Zhou, A. | |||||||||
![]() | ![]() Title: Allosteric Modulation of Hormone Release from Thyroxine and Corticosteroid Binding-Globulins. Authors: Qi, X. / Loiseau, F. / Chan, W.L. / Yan, Y. / Wei, Z. / Milroy, L.G. / Myers, R.M. / Ley, S.V. / Read, R.J. / Carrell, R.W. / Zhou, A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 170.6 KB | Display | ![]() |
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PDB format | ![]() | 132.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 19.7 KB | Display | |
Data in CIF | ![]() | 28.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2rivSC ![]() 2riwC ![]() 2xn3C ![]() 2xn5C ![]() 2xn6C 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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Unit cell |
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Components
-THYROXINE-BINDING ... , 2 types, 2 molecules AB
#1: Protein | Mass: 39145.879 Da / Num. of mol.: 1 / Fragment: RESIDUES 32-380 / Mutation: YES Source method: isolated from a genetically manipulated source Details: RESIDUES 346-355 OF TBG WERE REPLACED BY GAMFLEAIPRS Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 4026.811 Da / Num. of mol.: 1 / Fragment: RESIDUES 381-415 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Non-polymers , 5 types, 299 molecules ![](data/chem/img/T44.gif)
![](data/chem/img/F6Z.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/F6Z.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-T44 / | ||||
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#4: Chemical | ChemComp-F6Z / | ||||
#5: Chemical | #6: Chemical | ChemComp-CA / | #7: Water | ChemComp-HOH / | |
-Details
Compound details | ENGINEERED RESIDUE IN CHAIN A, ALA 366 TO GLY ENGINEERED RESIDUE IN CHAIN A, VAL 367 TO ALA ...ENGINEERED |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 48 % / Description: NONE |
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Crystal grow | pH: 5.4 / Details: 20% PEG3350, PH 5.4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.998 Å / Relative weight: 1 |
Reflection | Resolution: 1.43→1.51 Å / Num. obs: 72973 / % possible obs: 99.2 % / Observed criterion σ(I): 2 / Redundancy: 3.5 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 8.5 |
Reflection shell | Resolution: 1.43→1.51 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 2 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2RIV Resolution: 1.43→87.01 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.951 / SU B: 2.654 / SU ML: 0.047 / Cross valid method: THROUGHOUT / ESU R: 0.069 / ESU R Free: 0.068 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE FLUORESCEIN MOIETY OF THE THYROXINE-FLUORESCEIN (T4-5- CF) HAS LITTLE ELECTRON DENSITY, BUT IS MODELED STEREOCHEMICALLY AND INCLUDED IN THE REFINEMENT.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.881 Å2
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Refinement step | Cycle: LAST / Resolution: 1.43→87.01 Å
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Refine LS restraints |
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