+Open data
-Basic information
Entry | Database: PDB / ID: 6hfo | ||||||
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Title | Human Hsp90 co-chaperone TTC4 C-domain | ||||||
Components | Tetratricopeptide repeat protein 4 | ||||||
Keywords | CHAPERONE / unique fold / wheel domain / Hsp90 co-chaperone | ||||||
Function / homology | Function and homology information Hsp90 protein binding / defense response to virus / innate immune response / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.65 Å | ||||||
Authors | Huber, E.M. / Groll, M. | ||||||
Funding support | Germany, 1items
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Citation | Journal: Mol.Cell / Year: 2019 Title: The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2. Authors: Schopf, F.H. / Huber, E.M. / Dodt, C. / Lopez, A. / Biebl, M.M. / Rutz, D.A. / Muhlhofer, M. / Richter, G. / Madl, T. / Sattler, M. / Groll, M. / Buchner, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6hfo.cif.gz | 82.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6hfo.ent.gz | 61.7 KB | Display | PDB format |
PDBx/mmJSON format | 6hfo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6hfo_validation.pdf.gz | 429.3 KB | Display | wwPDB validaton report |
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Full document | 6hfo_full_validation.pdf.gz | 429.8 KB | Display | |
Data in XML | 6hfo_validation.xml.gz | 8.7 KB | Display | |
Data in CIF | 6hfo_validation.cif.gz | 11.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hf/6hfo ftp://data.pdbj.org/pub/pdb/validation_reports/hf/6hfo | HTTPS FTP |
-Related structure data
Related structure data | 6hfmSC 6hftC 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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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 19622.049 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TTC4, My044 / Production host: Escherichia coli (E. coli) / References: UniProt: O95801 |
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#2: Chemical | ChemComp-PO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.6 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: 1.4 M Na/K phosphate pH 8.2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID30B / Wavelength: 0.97856 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 5, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97856 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→45 Å / Num. obs: 20421 / % possible obs: 97.7 % / Redundancy: 3 % / Rmerge(I) obs: 0.044 / Net I/σ(I): 12.8 |
Reflection shell | Resolution: 1.65→1.75 Å / Rmerge(I) obs: 0.577 / Mean I/σ(I) obs: 1.9 / % possible all: 97.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6HFM Resolution: 1.65→15 Å / Cor.coef. Fo:Fc: 0.975 / Cor.coef. Fo:Fc free: 0.967 / SU B: 4.38 / SU ML: 0.064 / Cross valid method: THROUGHOUT / ESU R: 0.117 / ESU R Free: 0.085 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 42.755 Å2
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Refinement step | Cycle: 1 / Resolution: 1.65→15 Å
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Refine LS restraints |
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