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Open data
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Basic information
Entry | Database: PDB / ID: 4cv4 | ||||||
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Title | PIH N-terminal domain | ||||||
![]() | PIH1 DOMAIN-CONTAINING PROTEIN 1 | ||||||
![]() | CHAPERONE / PHOSPHORYLATION | ||||||
Function / homology | ![]() TORC1 complex assembly / snoRNA localization / positive regulation of glucose mediated signaling pathway / pre-snoRNP complex / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / R2TP complex / RPAP3/R2TP/prefoldin-like complex / box C/D snoRNP assembly / positive regulation of TORC1 signaling / epithelial cell differentiation ...TORC1 complex assembly / snoRNA localization / positive regulation of glucose mediated signaling pathway / pre-snoRNP complex / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / R2TP complex / RPAP3/R2TP/prefoldin-like complex / box C/D snoRNP assembly / positive regulation of TORC1 signaling / epithelial cell differentiation / histone reader activity / phosphoprotein binding / rRNA processing / histone binding / ATPase binding / chromatin remodeling / ribonucleoprotein complex / nucleolus / protein kinase binding / nucleus / 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. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 67.1 KB | Display | ![]() |
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PDB format | ![]() | 49.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 422.7 KB | Display | ![]() |
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Full document | ![]() | 423.6 KB | Display | |
Data in XML | ![]() | 9.6 KB | Display | |
Data in CIF | ![]() | 13.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4cguC ![]() 4cgvC ![]() 4cgwC ![]() 4chhC ![]() 4cktSC ![]() 4cseC 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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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 14976.923 Da / Num. of mol.: 1 / Fragment: RESIDUES 47-179 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-CO / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.87 Å3/Da / Density % sol: 34.42 % / Description: NONE |
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Crystal grow | pH: 7 Details: 0.02M MAGNESIUM CHLORIDE HEXAHYDRATE, 0.002M COBALT (2) CHLORIDE, 0.05M HEPES PH 7.5, 2M AMMONIUM SULFATE, 0.001M SPERMINE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: SATURN / Detector: CCD / Date: Mar 1, 2013 / Details: VARIMAX-HF MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54187 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→34.25 Å / Num. obs: 8928 / % possible obs: 98.1 % / Observed criterion σ(I): 2 / Redundancy: 4.3 % / Biso Wilson estimate: 10.63 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 22.7 |
Reflection shell | Resolution: 1.9→2.16 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 14.9 / % possible all: 96.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4CKT Resolution: 1.902→34.249 Å / SU ML: 0.13 / σ(F): 1.35 / Phase error: 15.98 / 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 | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 13.7 Å2 | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.902→34.249 Å
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Refine LS restraints |
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LS refinement shell |
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