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Open data
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Basic information
| Entry | Database: PDB / ID: 3ly5 | ||||||
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| Title | DDX18 dead-domain | ||||||
Components | ATP-dependent RNA helicase DDX18 | ||||||
Keywords | HYDROLASE / alpha-beta / Structural Genomics / Structural Genomics Consortium / SGC / ATP-binding / Helicase / Nucleotide-binding / RNA-binding | ||||||
| Function / homology | Function and homology informationmaturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / cellular response to estradiol stimulus / chromosome / RNA helicase activity / RNA helicase / nucleolus / ATP hydrolysis activity / RNA binding / ATP binding / membrane Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Schutz, P. / Karlberg, T. / Arrowsmith, C.H. / Berglund, H. / Bountra, C. / Collins, R. / Edwards, A.M. / Flodin, S. / Flores, A. / Graslund, S. ...Schutz, P. / Karlberg, T. / Arrowsmith, C.H. / Berglund, H. / Bountra, C. / Collins, R. / Edwards, A.M. / Flodin, S. / Flores, A. / Graslund, S. / Hammarstrom, M. / Johansson, A. / Johansson, I. / Kallas, A. / Kraulis, P. / Kotenyova, T. / Kotzsch, A. / Markova, N. / Moche, M. / Nielsen, T.K. / Nordlund, P. / Nyman, T. / Persson, C. / Roos, A.K. / Siponen, M.I. / Svensson, L. / Thorsell, A.G. / Tresaugues, L. / Van Den Berg, S. / Wahlberg, E. / Weigelt, J. / Welin, M. / Wisniewska, M. / Schuler, H.M. / Structural Genomics Consortium (SGC) | ||||||
Citation | Journal: Plos One / Year: 2010Title: 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: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 3ly5.cif.gz | 91.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3ly5.ent.gz | 67 KB | Display | PDB format |
| PDBx/mmJSON format | 3ly5.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ly/3ly5 ftp://data.pdbj.org/pub/pdb/validation_reports/ly/3ly5 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 2g9nC ![]() 2p6nC ![]() 2pl3C ![]() 2rb4C ![]() 3b7gC ![]() 3berC ![]() 3borC ![]() 3dkpC ![]() 3fe2C ![]() 3iuyC 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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Components
| #1: Protein | Mass: 29195.646 Da / Num. of mol.: 2 / Fragment: DEAD-domain, residues 149-387 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DDX18 / Plasmid: pNIC-Bsa4 / Production host: ![]() References: UniProt: Q9NVP1, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides #2: Chemical | ChemComp-PO4 / | #3: Chemical | #4: Chemical | #5: 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: 1.95 Å3/Da / Density % sol: 36.85 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.6 Details: 0.1 M HEPES pH 6.6, 0.2 M sodium thiocyanate, 20% w/v PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9789 Å |
| Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Sep 24, 2009 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9789 Å / Relative weight: 1 |
| Reflection | Resolution: 2.7→76.847 Å / Num. all: 12190 / Num. obs: 12190 / % possible obs: 100 % / Redundancy: 5.1 % / Rsym value: 0.213 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.8→38.42 Å / Cor.coef. Fo:Fc: 0.907 / Cor.coef. Fo:Fc free: 0.898 / Occupancy max: 1 / Occupancy min: 1 / SU B: 16.698 / SU ML: 0.343 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.428 / Stereochemistry target values: MAXIMUM LIKELIHOODDetails: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS; U VALUES: REFINED INDIVIDUALLY
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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 max: 61.15 Å2 / Biso mean: 46.29 Å2 / Biso min: 12.97 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.8→38.42 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 2.8→2.873 Å / Total num. of bins used: 20
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Homo sapiens (human)
X-RAY DIFFRACTION
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