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Open data
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Basic information
| Entry | Database: PDB / ID: 4wxa | ||||||
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| Title | Crystal structure of binary complex Gon7-Pcc1 | ||||||
Components |
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Keywords | TRANSCRIPTION / KEOPS / binary complex / Gon7-Pcc1 / tRNA t6A | ||||||
| Function / homology | Function and homology informationcellular response to pheromone / tRNA threonylcarbamoyladenosine metabolic process / EKC/KEOPS complex / tRNA threonylcarbamoyladenosine modification / cell wall mannoprotein biosynthetic process / telomere maintenance via recombination / telomere maintenance / maintenance of translational fidelity / chromatin DNA binding / molecular adaptor activity ...cellular response to pheromone / tRNA threonylcarbamoyladenosine metabolic process / EKC/KEOPS complex / tRNA threonylcarbamoyladenosine modification / cell wall mannoprotein biosynthetic process / telomere maintenance via recombination / telomere maintenance / maintenance of translational fidelity / chromatin DNA binding / molecular adaptor activity / chromosome, telomeric region / chromatin / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.44 Å | ||||||
Authors | Zhang, W. / van Tilbeurgh, H. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2015Title: Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex. Authors: Zhang, W. / Collinet, B. / Graille, M. / Daugeron, M.C. / Lazar, N. / Libri, D. / Durand, D. / van Tilbeurgh, 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 | 4wxa.cif.gz | 178.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb4wxa.ent.gz | 142.6 KB | Display | PDB format |
| PDBx/mmJSON format | 4wxa.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4wxa_validation.pdf.gz | 492.8 KB | Display | wwPDB validaton report |
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| Full document | 4wxa_full_validation.pdf.gz | 495.2 KB | Display | |
| Data in XML | 4wxa_validation.xml.gz | 16.4 KB | Display | |
| Data in CIF | 4wxa_validation.cif.gz | 22.8 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wx/4wxa ftp://data.pdbj.org/pub/pdb/validation_reports/wx/4wxa | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 4ww5C ![]() 4ww7C ![]() 4ww9C ![]() 4wwaC ![]() 4wx8C ![]() 4xahC 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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| 4 | ![]()
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| Unit cell |
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| Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
NCS oper:
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Components
| #1: Protein | Mass: 10834.401 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: PCC1, YKR095W-A Production host: ![]() References: UniProt: Q3E833 #2: Protein | Mass: 13623.011 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: GON7, LDB6, PCC2, YJL184W, J0420 Production host: ![]() References: UniProt: P46984 #3: Chemical | ChemComp-GOL / | #4: Chemical | ChemComp-ACT / | #5: Water | ChemComp-HOH / | Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.77 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.1 M Sodium Acetate pH 6.5, 20% PEG1500, 20% Glycerol, 3% Methanol PH range: 6.0 - 7.0 |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 2 / Wavelength: 0.9801 Å |
| Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: May 24, 2013 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9801 Å / Relative weight: 1 |
| Reflection | Resolution: 2.44→44.28 Å / Num. all: 94329 / Num. obs: 25516 / % possible obs: 99.11 % / Redundancy: 3.69 % / Net I/σ(I): 14.69 |
| Reflection shell | Resolution: 2.443→2.53 Å / % possible all: 94.59 |
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Processing
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| Refinement | Resolution: 2.44→44.28 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.924 / SU B: 21.586 / SU ML: 0.226 / Cross valid method: THROUGHOUT / ESU R: 0.296 / ESU R Free: 0.245 / 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: 64.221 Å2
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| Refinement step | Cycle: 1 / Resolution: 2.44→44.28 Å
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| Refine LS restraints |
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