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Yorodumi- PDB-3vke: Contribution of the first K-homology domain of poly(C)-binding pr... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3vke | ||||||
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Title | Contribution of the first K-homology domain of poly(C)-binding protein 1 to its affinity and specificity for C-rich oligonucleotides | ||||||
Components |
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Keywords | DNA BINDING PROTEIN/DNA / PCBP-1 / DNA RNA BINDING PROTEIN / KH DOMAIN / DNA BINDING PROTEIN-DNA complex | ||||||
Function / homology | Function and homology information sequence-specific single stranded DNA binding / Processing of Capped Intron-Containing Pre-mRNA / mRNA Splicing - Major Pathway / cytoplasmic ribonucleoprotein granule / single-stranded DNA binding / postsynaptic density / DNA-binding transcription factor activity, RNA polymerase II-specific / nuclear speck / cadherin binding / ribonucleoprotein complex ...sequence-specific single stranded DNA binding / Processing of Capped Intron-Containing Pre-mRNA / mRNA Splicing - Major Pathway / cytoplasmic ribonucleoprotein granule / single-stranded DNA binding / postsynaptic density / DNA-binding transcription factor activity, RNA polymerase II-specific / nuclear speck / cadherin binding / ribonucleoprotein complex / viral RNA genome replication / mRNA binding / positive regulation of transcription by RNA polymerase II / RNA binding / extracellular exosome / nucleoplasm / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.77 Å | ||||||
Authors | Traore, D.A.K. / Wilce, M.C.J. / Wilce, J.A. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2012 Title: Contribution of the first K-homology domain of poly(C)-binding protein 1 to its affinity and specificity for C-rich oligonucleotides Authors: Yoga, Y.M.K. / Traore, D.A.K. / Sidiqi, M. / Szeto, C. / Pendini, N.R. / Barker, A. / Leedman, P.J. / Wilce, J.A. / Wilce, M.C.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3vke.cif.gz | 147.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3vke.ent.gz | 116.6 KB | Display | PDB format |
PDBx/mmJSON format | 3vke.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vk/3vke ftp://data.pdbj.org/pub/pdb/validation_reports/vk/3vke | HTTPS FTP |
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-Related structure data
Related structure data | 1ztgSC 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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3 |
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4 |
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Unit cell |
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-Components
#1: Protein | Mass: 8462.802 Da / Num. of mol.: 4 / Fragment: KH1 domain / Mutation: C54S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PCBP1 / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q15365 #2: DNA chain | Mass: 1738.183 Da / Num. of mol.: 4 / Source method: obtained synthetically #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: 2.35 Å3/Da / Density % sol: 47.77 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.2 Details: 0.1M phosphate-citrate, 40%(v/v) PEG 300, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 0.9801 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 5, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9801 Å / Relative weight: 1 |
Reflection | Resolution: 1.77→38.51 Å / Num. obs: 36143 / Observed criterion σ(I): 3 / Redundancy: 3.2 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 7.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1ZTG Resolution: 1.77→27.16 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.944 / Occupancy max: 1 / Occupancy min: 0 / SU B: 4.484 / SU ML: 0.065 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.145 / ESU R Free: 0.107 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: 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: 90.59 Å2 / Biso mean: 31.5288 Å2 / Biso min: 13.06 Å2
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Refinement step | Cycle: LAST / Resolution: 1.77→27.16 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.77→1.816 Å / Total num. of bins used: 20
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