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Yorodumi- PDB-7e2e: Crystal structure of the Estrogen-Related Receptor alpha (ERRalph... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7e2e | ||||||
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Title | Crystal structure of the Estrogen-Related Receptor alpha (ERRalpha) ligand-binding domain (LBD) in complex with an agonist DS45500853 and a PGC-1alpha peptide | ||||||
Components |
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Keywords | TRANSCRIPTION / Nuclear receptor / Complex / agonist | ||||||
Function / homology | Function and homology information positive regulation of mitochondrial DNA metabolic process / positive regulation of muscle tissue development / positive regulation of cellular respiration / positive regulation of fatty acid oxidation / : / : / lncRNA binding / response to muscle activity / cellular respiration / Activation of PPARGC1A (PGC-1alpha) by phosphorylation ...positive regulation of mitochondrial DNA metabolic process / positive regulation of muscle tissue development / positive regulation of cellular respiration / positive regulation of fatty acid oxidation / : / : / lncRNA binding / response to muscle activity / cellular respiration / Activation of PPARGC1A (PGC-1alpha) by phosphorylation / temperature homeostasis / nuclear steroid receptor activity / intercellular bridge / positive regulation of ATP biosynthetic process / response to starvation / intracellular glucose homeostasis / fatty acid oxidation / response to dietary excess / estrogen response element binding / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / adipose tissue development / energy homeostasis / brown fat cell differentiation / intracellular steroid hormone receptor signaling pathway / positive regulation of gluconeogenesis / digestion / respiratory electron transport chain / steroid binding / mitochondrion organization / RNA splicing / SUMOylation of transcription cofactors / nuclear receptor coactivator activity / gluconeogenesis / transcription initiation at RNA polymerase II promoter / nuclear receptor binding / negative regulation of smooth muscle cell proliferation / transcription coregulator activity / circadian regulation of gene expression / Heme signaling / Transcriptional activation of mitochondrial biogenesis / regulation of circadian rhythm / PPARA activates gene expression / chromatin DNA binding / fibrillar center / PML body / mRNA processing / positive regulation of DNA-binding transcription factor activity / Transcriptional regulation of white adipocyte differentiation / Nuclear Receptor transcription pathway / Regulation of RUNX2 expression and activity / nuclear receptor activity / microtubule cytoskeleton / sequence-specific double-stranded DNA binding / Circadian Clock / positive regulation of cold-induced thermogenesis / cellular response to oxidative stress / protein-containing complex assembly / neuron apoptotic process / DNA-binding transcription factor binding / RNA polymerase II-specific DNA-binding transcription factor binding / negative regulation of neuron apoptotic process / sequence-specific DNA binding / transcription coactivator activity / protein stabilization / DNA-binding transcription factor activity, RNA polymerase II-specific / DNA-binding transcription factor activity / protein domain specific binding / ubiquitin protein ligase binding / chromatin / regulation of DNA-templated transcription / positive regulation of gene expression / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / DNA binding / RNA binding / zinc ion binding / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.7 Å | ||||||
Authors | Ito, S. / Shinozuka, T. / Kimura, T. / Izumi, M. / Wakabayashi, K. | ||||||
Citation | Journal: Acs Med.Chem.Lett. / Year: 2021 Title: Discovery of a Novel Class of ERR alpha Agonists. Authors: Shinozuka, T. / Ito, S. / Kimura, T. / Izumi, M. / Wakabayashi, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7e2e.cif.gz | 190.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7e2e.ent.gz | 152.4 KB | Display | PDB format |
PDBx/mmJSON format | 7e2e.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e2/7e2e ftp://data.pdbj.org/pub/pdb/validation_reports/e2/7e2e | HTTPS FTP |
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-Related structure data
Related structure data | 1xb7S S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
NCS oper:
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-Components
#1: Protein | Mass: 26894.053 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ESRRA, ERR1, ESRL1, NR3B1 / Production host: Escherichia coli (E. coli) / References: UniProt: P11474 #2: Protein/peptide | Mass: 1393.628 Da / Num. of mol.: 2 / Mutation: C207A / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q9UBK2 #3: Chemical | #4: Chemical | ChemComp-IOD / | #5: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 43.97 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7.6 Details: 18% (v/v) PEG 3350, 0.2 M NaI, 0.1 M HEPES (pH 7.6) |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NW12A / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Feb 2, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→40 Å / Num. obs: 13464 / % possible obs: 99.7 % / Redundancy: 7.2 % / Rmerge(I) obs: 0.086 / Net I/σ(I): 23.1 |
Reflection shell | Resolution: 2.7→2.75 Å / Rmerge(I) obs: 0.443 / Mean I/σ(I) obs: 3.8 / Num. unique obs: 685 |
-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1XB7 Resolution: 2.7→20 Å / Cor.coef. Fo:Fc: 0.922 / Cor.coef. Fo:Fc free: 0.887 / SU B: 34.63 / SU ML: 0.367 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.468 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: U VALUES : WITH TLS ADDED
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 138.6 Å2 / Biso mean: 67.608 Å2 / Biso min: 30.92 Å2
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Refinement step | Cycle: final / Resolution: 2.7→20 Å
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Refine LS restraints |
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Refine LS restraints NCS | Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 2.7→2.769 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin y: 66.878 Å / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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