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Yorodumi- PDB-3b7g: Human DEAD-box RNA helicase DDX20, Conserved domain I (DEAD) in c... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3b7g | ||||||
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Title | Human DEAD-box RNA helicase DDX20, Conserved domain I (DEAD) in complex with AMPPNP (Adenosine-(Beta,gamma)-imidotriphosphate) | ||||||
Components | Probable ATP-dependent RNA helicase DDX20 | ||||||
Keywords | HYDROLASE / RNA / HELICASE / DEAD / CONSERVED DOMAIN I / STRUCTURAL GENOMICS / STRUCTURAL GENOMICS CONSORTIUM / SGC / ATP-binding / DNA-binding / mRNA processing / mRNA splicing / Nucleotide-binding / Nucleus / Phosphorylation / Spliceosome | ||||||
Function / homology | Function and homology information Gemini of coiled bodies / SMN complex / RNA polymerase II transcription repressor complex / regulation of steroid biosynthetic process / SMN-Sm protein complex / oogenesis / spliceosomal tri-snRNP complex assembly / spliceosomal snRNP assembly / RNA processing / histone deacetylase binding ...Gemini of coiled bodies / SMN complex / RNA polymerase II transcription repressor complex / regulation of steroid biosynthetic process / SMN-Sm protein complex / oogenesis / spliceosomal tri-snRNP complex assembly / spliceosomal snRNP assembly / RNA processing / histone deacetylase binding / nucleoside-triphosphate phosphatase / protein-macromolecule adaptor activity / snRNP Assembly / SARS-CoV-2 modulates host translation machinery / DNA-binding transcription factor binding / RNA helicase activity / nuclear body / cytoskeleton / RNA helicase / positive regulation of apoptotic process / protein domain specific binding / negative regulation of cell population proliferation / negative regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / RNA binding / nucleoplasm / ATP binding / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Karlberg, T. / Tresaugues, L. / Arrowsmith, C.H. / Berglund, H. / Busam, R.D. / Collins, R. / Dahlgren, L.G. / Edwards, A.M. / Flodin, S. / Flores, A. ...Karlberg, T. / Tresaugues, L. / Arrowsmith, C.H. / Berglund, H. / Busam, R.D. / Collins, R. / Dahlgren, L.G. / Edwards, A.M. / Flodin, S. / Flores, A. / Graslund, S. / Hammarstrom, M. / Johansson, I. / Kallas, A. / Kotenyova, T. / Lehtio, L. / Moche, M. / Nilsson, M.E. / Nordlund, P. / Nyman, T. / Persson, C. / Sagemark, J. / Svensson, L. / Thorsell, A.G. / Van Den Berg, S. / Weigelt, J. / Welin, M. / Holmberg-Schiavone, L. / Structural Genomics Consortium (SGC) | ||||||
Citation | Journal: Plos One / Year: 2010 Title: Comparative Structural Analysis of Human DEAD-Box RNA Helicases. Authors: Schutz, P. / Karlberg, T. / van den Berg, S. / Collins, R. / Lehtio, L. / Hogbom, M. / Holmberg-Schiavone, L. / Tempel, W. / Park, H.W. / Hammarstrom, M. / Moche, M. / Thorsell, A.G. / Schuler, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3b7g.cif.gz | 104.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3b7g.ent.gz | 79.9 KB | Display | PDB format |
PDBx/mmJSON format | 3b7g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b7/3b7g ftp://data.pdbj.org/pub/pdb/validation_reports/b7/3b7g | HTTPS FTP |
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-Related structure data
Related structure data | 2g9nC 2p6nC 2pl3C 2rb4C 3berC 3borC 3dkpC 3fe2C 3iuyC 3ly5C 2oxcS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: ALA / Beg label comp-ID: ALA / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: 5 / Auth seq-ID: 62 - 266 / Label seq-ID: 24 - 228
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-Components
#1: Protein | Mass: 25176.213 Da / Num. of mol.: 2 / Fragment: DEAD domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DDX20, DP103, GEMIN3 / Plasmid: pNIC-Bsa4 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)gold pRARE2 References: UniProt: Q9UHI6, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.51 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: 25% PEG 3350, 200mM Ammonium acetate, 100mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1.00595 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 1, 2007 / Details: Mirrors |
Radiation | Monochromator: Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.00595 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→45 Å / Num. all: 40642 / Num. obs: 40642 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 20.5 % / Rmerge(I) obs: 0.081 / Rsym value: 0.023 / Net I/σ(I): 32.1 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 18.2 % / Rmerge(I) obs: 0.126 / Mean I/σ(I) obs: 21.3 / Num. unique all: 5705 / Rsym value: 0.041 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 2OXC Resolution: 1.9→38.43 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.926 / SU B: 4.338 / SU ML: 0.069 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.13 / ESU R Free: 0.12 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: 14.938 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→38.43 Å
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Refine LS restraints |
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Refine LS restraints NCS | Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 1.9→1.949 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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