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- PDB-6brg: The SAM domain of mouse SAMHD1 is critical for its activation and... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6brg | ||||||
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Title | The SAM domain of mouse SAMHD1 is critical for its activation and regulation | ||||||
![]() | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 | ||||||
![]() | HYDROLASE / dNTPase / Allosteric Regulation / Binding Sites / Mouse / Models / Molecular / Protein Conformation / Protein Multimerization | ||||||
Function / homology | ![]() Nucleotide catabolism / Hydrolases; Acting on ester bonds; Triphosphoric-monoester hydrolases / deoxynucleoside triphosphate hydrolase activity / triphosphoric monoester hydrolase activity / dGTP binding / dATP catabolic process / dGTPase activity / tetraspanin-enriched microdomain / DNA strand resection involved in replication fork processing / deoxyribonucleotide catabolic process ...Nucleotide catabolism / Hydrolases; Acting on ester bonds; Triphosphoric-monoester hydrolases / deoxynucleoside triphosphate hydrolase activity / triphosphoric monoester hydrolase activity / dGTP binding / dATP catabolic process / dGTPase activity / tetraspanin-enriched microdomain / DNA strand resection involved in replication fork processing / deoxyribonucleotide catabolic process / dGTP catabolic process / negative regulation of type I interferon-mediated signaling pathway / regulation of innate immune response / somatic hypermutation of immunoglobulin genes / double-strand break repair via homologous recombination / site of double-strand break / single-stranded DNA binding / protein homotetramerization / defense response to virus / nucleic acid binding / innate immune response / DNA damage response / GTP binding / RNA binding / zinc ion binding / nucleoplasm / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Buzovetsky, O. / Tang, C. / Knecht, K.M. / Antonucci, J.M. / Wu, L. / Ji, X. / Xiong, Y. | ||||||
![]() | ![]() Title: The SAM domain of mouse SAMHD1 is critical for its activation and regulation. Authors: Buzovetsky, O. / Tang, C. / Knecht, K.M. / Antonucci, J.M. / Wu, L. / Ji, X. / Xiong, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 844.5 KB | Display | ![]() |
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PDB format | ![]() | 703.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 473.2 KB | Display | ![]() |
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Full document | ![]() | 490.5 KB | Display | |
Data in XML | ![]() | 65.6 KB | Display | |
Data in CIF | ![]() | 89.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6brhC ![]() 6brkC ![]() 5ajaS S: Starting model for refinement 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Beg auth comp-ID: THR / Beg label comp-ID: THR / End auth comp-ID: GLN / End label comp-ID: GLN / Refine code: _ / Auth seq-ID: 72 - 624 / Label seq-ID: 86 - 638
NCS ensembles :
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Components
#1: Protein | Mass: 77546.781 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-MG / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.92 % |
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Crystal grow | Temperature: 298 K / Method: batch mode / pH: 7.4 / Details: 100 mM SPG (Qiagen) buffer, pH 7.4, 25% PEG 1500 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Dec 14, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97918 Å / Relative weight: 1 |
Reflection | Resolution: 3.5→50 Å / Num. obs: 34596 / % possible obs: 98.8 % / Redundancy: 2.4 % / Rmerge(I) obs: 0.15 / Net I/σ(I): 6.4 |
Reflection shell | Resolution: 3.5→3.56 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5AJA Resolution: 3.5→20 Å / Cor.coef. Fo:Fc: 0.89 / Cor.coef. Fo:Fc free: 0.856 / SU B: 100.187 / SU ML: 0.663 / Cross valid method: THROUGHOUT / ESU R Free: 0.706
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 89.157 Å2
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Refinement step | Cycle: 1 / Resolution: 3.5→20 Å
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Refine LS restraints |
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