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- PDB-4w9q: The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-[(3,5-dich... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4w9q | ||||||
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Title | The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-[(3,5-dichlorophenyl)sulfonyl]-3-[2-(3,4-dimethoxyphenoxy)ethyl]-5-ethyl-3,10-diazabicyclo[4.3.1]decan-2-one | ||||||
![]() | Peptidyl-prolyl cis-trans isomerase FKBP5 | ||||||
![]() | ISOMERASE / Fk-506 binding domain / Hsp90 cochaperone / immunophiline / peptidyl-prolyl isomerase / ligand selectivity | ||||||
Function / homology | ![]() FK506 binding / chaperone-mediated protein folding / MECP2 regulates neuronal receptors and channels / heat shock protein binding / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / ESR-mediated signaling / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / response to bacterium / protein folding ...FK506 binding / chaperone-mediated protein folding / MECP2 regulates neuronal receptors and channels / heat shock protein binding / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / ESR-mediated signaling / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / response to bacterium / protein folding / protein-macromolecule adaptor activity / extracellular exosome / nucleoplasm / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Pomplun, S. / Wang, Y. / Kirschner, K. / Kozany, C. / Bracher, A. / Hausch, F. | ||||||
![]() | ![]() Title: Rational Design and Asymmetric Synthesis of Potent and Neurotrophic Ligands for FK506-Binding Proteins (FKBPs). Authors: Pomplun, S. / Wang, Y. / Kirschner, A. / Kozany, C. / Bracher, A. / Hausch, F. #1: ![]() Title: Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90 Authors: Bracher, A. / Kozany, C. / Thost, A.-K. / Hausch, F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 77.4 KB | Display | ![]() |
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PDB format | ![]() | 55.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 763.6 KB | Display | ![]() |
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Full document | ![]() | 765.7 KB | Display | |
Data in XML | ![]() | 10.4 KB | Display | |
Data in CIF | ![]() | 15 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4w9oC ![]() 4w9pC ![]() 3o5qS S: Starting model for refinement 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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Details | biological unit is a monomer |
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Components
#1: Protein | Mass: 14026.077 Da / Num. of mol.: 1 / Fragment: Fk1 domain, UNP residues 16-140 / Mutation: yes Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-3JP / ( |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47.09 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 37 % PEG-3350, 8 % DMSO, 2 mM ligand, 0.2 M NH4-acetate and 0.1 M HEPES-NaOH pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 14, 2010 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.8 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.08→56.779 Å / Num. all: 53393 / Num. obs: 53393 / % possible obs: 94.2 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.062 / Rpim(I) all: 0.037 / Rrim(I) all: 0.072 / Rsym value: 0.062 / Net I/av σ(I): 5.385 / Net I/σ(I): 10.5 / Num. measured all: 192898 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: _
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3O5Q Resolution: 1.08→20 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.969 / WRfactor Rfree: 0.181 / WRfactor Rwork: 0.1556 / FOM work R set: 0.9247 / SU B: 0.754 / SU ML: 0.017 / SU R Cruickshank DPI: 0.0306 / SU Rfree: 0.0302 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.031 / ESU R Free: 0.03 / 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 max: 36.93 Å2 / Biso mean: 8.146 Å2 / Biso min: 5.24 Å2
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Refinement step | Cycle: final / Resolution: 1.08→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.08→1.108 Å / Total num. of bins used: 20
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