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Yorodumi- PDB-2e8p: Solution structure of the N-terminal SAM-domain of E74-like factor 3 -
+Open data
-Basic information
Entry | Database: PDB / ID: 2e8p | ||||||
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Title | Solution structure of the N-terminal SAM-domain of E74-like factor 3 | ||||||
Components | ELF3 protein | ||||||
Keywords | SIGNALING PROTEIN / CELL-FREE PROTEIN SYNTHESIS / PROTEIN REGULATION / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information mammary gland involution / chromatin => GO:0000785 / positive regulation of Notch signaling pathway / blastocyst development / epithelial cell differentiation / extracellular matrix organization / Pre-NOTCH Transcription and Translation / sequence-specific double-stranded DNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / transcription by RNA polymerase II ...mammary gland involution / chromatin => GO:0000785 / positive regulation of Notch signaling pathway / blastocyst development / epithelial cell differentiation / extracellular matrix organization / Pre-NOTCH Transcription and Translation / sequence-specific double-stranded DNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / transcription by RNA polymerase II / cell differentiation / DNA-binding transcription factor activity, RNA polymerase II-specific / inflammatory response / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of DNA-templated transcription / host cell nucleus / regulation of transcription by RNA polymerase II / Golgi apparatus / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Goroncy, A.K. / Sato, M. / Koshiba, S. / Watanabe, S. / Harada, T. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the N-terminal SAM-domain of E74-like factor 3 Authors: Goroncy, A.K. / Sato, M. / Koshiba, S. / Watanabe, S. / Harada, T. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2e8p.cif.gz | 535.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2e8p.ent.gz | 449.9 KB | Display | PDB format |
PDBx/mmJSON format | 2e8p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2e8p_validation.pdf.gz | 338.9 KB | Display | wwPDB validaton report |
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Full document | 2e8p_full_validation.pdf.gz | 451.7 KB | Display | |
Data in XML | 2e8p_validation.xml.gz | 25.4 KB | Display | |
Data in CIF | 2e8p_validation.cif.gz | 41.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e8/2e8p ftp://data.pdbj.org/pub/pdb/validation_reports/e8/2e8p | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10130.163 Da / Num. of mol.: 1 / Fragment: SAM domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: CELL-FREE PROTEIN SYNTHESIS / Gene: ELF3 / Plasmid: P060313-01 / References: UniProt: Q6IAP8, UniProt: P78545*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.18mM SAM DOMAIN, 20mM d-TRIS-HCL, 100mM NaCl, 1mM d-DTT, 0.02% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.0 / Pressure: AMBIENT / Temperature: 296 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |