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Open data
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Basic information
Entry | Database: PDB / ID: 4ckt | ||||||
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Title | PIH1 N-terminal domain | ||||||
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![]() | CHAPERONE/PEPTIDE / CHAPERONE-PEPTIDE COMPLEX / CHAPERONE / MULTIPROTEIN COMPLEXES / PHOSPHORYLATION / R2TP | ||||||
Function / homology | ![]() protein-containing complex stabilizing activity / : / TTT Hsp90 cochaperone complex / TORC1 complex assembly / positive regulation of TORC2 signaling / snoRNA localization / positive regulation of glucose mediated signaling pathway / pre-snoRNP complex / TORC2 complex / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I ...protein-containing complex stabilizing activity / : / TTT Hsp90 cochaperone complex / TORC1 complex assembly / positive regulation of TORC2 signaling / snoRNA localization / positive regulation of glucose mediated signaling pathway / pre-snoRNP complex / TORC2 complex / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / TORC1 complex / R2TP complex / regulation of TOR signaling / RPAP3/R2TP/prefoldin-like complex / box C/D snoRNP assembly / telomeric DNA binding / telomere maintenance via telomerase / epithelial cell differentiation / positive regulation of TORC1 signaling / histone reader activity / nuclear periphery / phosphoprotein binding / Hsp90 protein binding / kinase binding / rRNA processing / histone binding / ATPase binding / chromosome, telomeric region / molecular adaptor activity / nuclear body / protein stabilization / ribonucleoprotein complex / chromatin remodeling / protein-containing complex binding / nucleolus / protein kinase binding / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Morgan, R.M. / Roe, S.M. | ||||||
![]() | ![]() Title: Structural Basis for Phosphorylation-Dependent Recruitment of Tel2 to Hsp90 by Pih1. Authors: Pal, M. / Morgan, M. / Phelps, S.E. / Roe, S.M. / Parry-Morris, S. / Downs, J.A. / Polier, S. / Pearl, L.H. / Prodromou, C. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 61.5 KB | Display | ![]() |
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PDB format | ![]() | 49.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4cguC ![]() 4cgvC ![]() 4cgwC ![]() 4chhC ![]() 4cseC ![]() 4cv4C 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 22600.400 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-200 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein/peptide | Mass: 1135.973 Da / Num. of mol.: 2 / Fragment: RESIDUES 489-496 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.88 Å3/Da / Density % sol: 34.59 % / Description: NONE |
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Crystal grow | pH: 7 / Details: pH 7 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 30, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 3.06→61.67 Å / Num. obs: 68364 / % possible obs: 90.1 % / Observed criterion σ(I): 0 / Redundancy: 10.8 % / Biso Wilson estimate: 62.28 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 3.06→3.14 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 2.5 / % possible all: 56.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 3→54.599 Å / SU ML: 0.41 / σ(F): 1.91 / Phase error: 28.68 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→54.599 Å
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Refine LS restraints |
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LS refinement shell |
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