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- PDB-1r20: Crystal structure of the ligand-binding domains of the heterodime... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1r20 | ||||||
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Title | Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830 | ||||||
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![]() | hormone/growth factor receptor / NUCLEAR RECEPTOR / HETERODIMER / ALPHA-HELICAL SANDWICH / Structural Proteomics in Europe / SPINE / Structural Genomics / hormone-growth factor receptor COMPLEX | ||||||
Function / homology | ![]() ecdysone binding / ecdysone receptor signaling pathway / bile acid signaling pathway / nuclear steroid receptor activity / negative regulation of inflammatory response / nuclear receptor activity / cell differentiation / RNA polymerase II cis-regulatory region sequence-specific DNA binding / regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II ...ecdysone binding / ecdysone receptor signaling pathway / bile acid signaling pathway / nuclear steroid receptor activity / negative regulation of inflammatory response / nuclear receptor activity / cell differentiation / RNA polymerase II cis-regulatory region sequence-specific DNA binding / regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / zinc ion binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Billas, I.M.L. / Iwema, T. / Garnier, J.M. / Mitschler, A. / Rochel, N. / Moras, D. / Structural Proteomics in Europe (SPINE) | ||||||
![]() | ![]() Title: Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor. Authors: Billas, I.M.L. / Iwema, T. / Garnier, J.M. / Mitschler, A. / Rochel, N. / Moras, D. | ||||||
History |
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Remark 999 | sequence no suitable sequence database reference was available for chains A or D, at the time of ...sequence no suitable sequence database reference was available for chains A or D, at the time of processing this file. In chain D the following residues were mutated compared to the wild- type protein: W303Y, A361S, L456S, C483S. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 108.7 KB | Display | ![]() |
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PDB format | ![]() | 83 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 24.6 KB | Display | |
Data in CIF | ![]() | 32.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 29951.760 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 30206.619 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Chemical | ChemComp-EPH / |
#4: Chemical | ChemComp-HWG / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.27 Å3/Da / Density % sol: 62.38 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 1000, PEG 8000, MgCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 24 ℃ / pH: 8 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength | Wavelength: 0.9393 Å / Relative weight: 1 | ||||||||||||||||||
Reflection | Resolution: 3→15 Å / Num. all: 15421 / Num. obs: 15421 / % possible obs: 95.3 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Rsym value: 0.072 | ||||||||||||||||||
Reflection shell | Resolution: 3→3.07 Å / Rsym value: 0.355 / % possible all: 85.6 | ||||||||||||||||||
Reflection | *PLUS Highest resolution: 3 Å / Redundancy: 8.3 % / Num. measured all: 127854 / Rmerge(I) obs: 0.072 | ||||||||||||||||||
Reflection shell | *PLUS Highest resolution: 3 Å / % possible obs: 85.6 % / Rmerge(I) obs: 0.355 / Mean I/σ(I) obs: 3.4 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 3→15 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 3 Å / % reflection Rfree: 10 % | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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