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- PDB-8vfk: Crystal Structure of Delta 109-117 D-Dopachrome Tautomerase (D-DT) -
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Open data
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Basic information
Entry | Database: PDB / ID: 8vfk | ||||||
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Title | Crystal Structure of Delta 109-117 D-Dopachrome Tautomerase (D-DT) | ||||||
![]() | D-dopachrome decarboxylase | ||||||
![]() | ISOMERASE / Truncation / Enzyme / Cytokine | ||||||
Function / homology | ![]() D-dopachrome decarboxylase / D-dopachrome decarboxylase activity / dopachrome isomerase activity / phenylpyruvate tautomerase activity / melanin biosynthetic process / cytokine receptor binding / negative regulation of macrophage chemotaxis / positive regulation of inflammatory response / positive regulation of tumor necrosis factor production / positive regulation of ERK1 and ERK2 cascade ...D-dopachrome decarboxylase / D-dopachrome decarboxylase activity / dopachrome isomerase activity / phenylpyruvate tautomerase activity / melanin biosynthetic process / cytokine receptor binding / negative regulation of macrophage chemotaxis / positive regulation of inflammatory response / positive regulation of tumor necrosis factor production / positive regulation of ERK1 and ERK2 cascade / extracellular space / extracellular exosome / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Parkins, A. / Pilien, A. / Wolff, A. / Thompson, M.C. / Pantouris, G. | ||||||
Funding support | 1items
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![]() | ![]() Title: The C-terminal Region of D-DT Regulates Molecular Recognition for Protein-Ligand Complexes. Authors: Parkins, A. / Pilien, A.V.R. / Wolff, A.M. / Argueta, C. / Vargas, J. / Sadeghi, S. / Franz, A.H. / Thompson, M.C. / Pantouris, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 77.3 KB | Display | ![]() |
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PDB format | ![]() | 57 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 448.5 KB | Display | ![]() |
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Full document | ![]() | 448.7 KB | Display | |
Data in XML | ![]() | 15.6 KB | Display | |
Data in CIF | ![]() | 22 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8vdyC ![]() 8vflC ![]() 8vfnC ![]() 8vfoC ![]() 8vfwC ![]() 8vg5C ![]() 8vg7C ![]() 8vg8C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 11601.270 Da / Num. of mol.: 3 / Mutation: Delta 109-117 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-NA / | #4: Water | ChemComp-HOH / | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.6 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop Details: 26-28% PEG 4000, 0.1M Sodium Citrate pH 6.0-6.2, 0.2M Ammonium Acetate PH range: 6.0-6.2 |
-Data collection
Diffraction | Mean temperature: 290 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jun 15, 2022 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.11583 Å / Relative weight: 1 |
Reflection | Resolution: 1.59→65.38 Å / Num. obs: 41389 / % possible obs: 98.5 % / Redundancy: 11.6 % / CC1/2: 0.993 / Rmerge(I) obs: 0.247 / Rpim(I) all: 0.075 / Rrim(I) all: 0.258 / Net I/σ(I): 4.9 / Num. measured all: 479440 |
Reflection shell | Resolution: 1.59→1.62 Å / % possible obs: 97.2 % / Redundancy: 11.8 % / Rmerge(I) obs: 1.875 / Num. measured all: 24220 / Num. unique obs: 2046 / CC1/2: 0.469 / Rpim(I) all: 0.56 / Rrim(I) all: 1.957 / Net I/σ(I) obs: 0.7 |
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Processing
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Refinement | Method to determine structure: ![]()
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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 mean: 19.454 Å2
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Refinement step | Cycle: 1 / Resolution: 1.59→65.38 Å
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Refine LS restraints |
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