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- PDB-6urq: Complex structure of human poly-ADP-ribosyltransferase TNKS1 ARC2... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6urq | ||||||
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Title | Complex structure of human poly-ADP-ribosyltransferase TNKS1 ARC2-ARC3 and P antigen family member 4 (PAGE4) | ||||||
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![]() | Transferase/Transcription / TNKS / PAGE4 / tankyrase / PARP / cancer-testis antigen / Wnt signaling / Transferase-Transcription complex | ||||||
Function / homology | ![]() : / negative regulation of telomeric DNA binding / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / regulation of telomere maintenance via telomerase / XAV939 stabilizes AXIN / NAD+ ADP-ribosyltransferase / negative regulation of telomere maintenance via telomere lengthening / protein auto-ADP-ribosylation / protein localization to chromosome, telomeric region / regulation of stress-activated MAPK cascade ...: / negative regulation of telomeric DNA binding / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / regulation of telomere maintenance via telomerase / XAV939 stabilizes AXIN / NAD+ ADP-ribosyltransferase / negative regulation of telomere maintenance via telomere lengthening / protein auto-ADP-ribosylation / protein localization to chromosome, telomeric region / regulation of stress-activated MAPK cascade / protein poly-ADP-ribosylation / pericentriolar material / mitotic spindle pole / response to starvation / NAD+-protein ADP-ribosyltransferase activity / positive regulation of telomere capping / Transferases; Glycosyltransferases; Pentosyltransferases / NAD+-protein poly-ADP-ribosyltransferase activity / mRNA transport / spindle assembly / nuclear pore / negative regulation of reactive oxygen species biosynthetic process / : / positive regulation of telomere maintenance via telomerase / nucleotidyltransferase activity / mitotic spindle organization / TCF dependent signaling in response to WNT / Degradation of AXIN / peptidyl-threonine phosphorylation / Wnt signaling pathway / Regulation of PTEN stability and activity / protein polyubiquitination / protein transport / positive regulation of canonical Wnt signaling pathway / histone binding / peptidyl-serine phosphorylation / nuclear membrane / response to oxidative stress / chromosome, telomeric region / transcription coactivator activity / nuclear body / Ub-specific processing proteases / cell division / Golgi membrane / negative regulation of apoptotic process / Golgi apparatus / positive regulation of transcription by RNA polymerase II / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Zheng, Y. / Koirala, S. / Miller, D. / Potts, P.R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Tissue-Specific Regulation of the Wnt/ beta-Catenin Pathway by PAGE4 Inhibition of Tankyrase. Authors: Koirala, S. / Klein, J. / Zheng, Y. / Glenn, N.O. / Eisemann, T. / Fon Tacer, K. / Miller, D.J. / Kulak, O. / Lu, M. / Finkelstein, D.B. / Neale, G. / Tillman, H. / Vogel, P. / Strand, D.W. ...Authors: Koirala, S. / Klein, J. / Zheng, Y. / Glenn, N.O. / Eisemann, T. / Fon Tacer, K. / Miller, D.J. / Kulak, O. / Lu, M. / Finkelstein, D.B. / Neale, G. / Tillman, H. / Vogel, P. / Strand, D.W. / Lum, L. / Brautigam, C.A. / Pascal, J.M. / Clements, W.K. / Potts, P.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 171.7 KB | Display | ![]() |
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PDB format | ![]() | 107.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 273.5 KB | Display | ![]() |
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Full document | ![]() | 273.5 KB | Display | |
Data in XML | ![]() | 1.3 KB | Display | |
Data in CIF | ![]() | 9.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3utmS 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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Unit cell |
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Components
#1: Protein | Mass: 34948.152 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: O95271, NAD+ ADP-ribosyltransferase, Transferases; Glycosyltransferases; Pentosyltransferases #2: Protein | Mass: 11170.020 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-SO4 / | #4: Chemical | ChemComp-GOL / | #5: 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: 2.66 Å3/Da / Density % sol: 53.73 % |
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Crystal grow | Temperature: 298 K / Method: evaporation / pH: 6 Details: 100 mM Ammonium Sulfate, 10 mM DTT, 100 mM MES pH 6.0, 7% w/v PEG4000, 1% 1,6-Hexanediol |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 8, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→39.75 Å / Num. obs: 60143 / % possible obs: 99.4 % / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Biso Wilson estimate: 33.24 Å2 / CC1/2: 0.996 / Rpim(I) all: 0.043 / Rrim(I) all: 0.085 / Rsym value: 0.073 / Net I/σ(I): 10.2 |
Reflection shell | Resolution: 2.05→2.1 Å / Redundancy: 3.8 % / Mean I/σ(I) obs: 2.1 / Num. unique obs: 4432 / Rpim(I) all: 0.422 / Rrim(I) all: 0.834 / Rsym value: 0.718 / % possible all: 98.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3UTM Resolution: 2.05→39.75 Å / SU ML: 0.2466 / Cross valid method: FREE R-VALUE / σ(F): 1.06 / Phase error: 26.0844 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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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 mean: 40.14 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.05→39.75 Å
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Refine LS restraints |
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LS refinement shell |
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