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Open data
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Basic information
| Entry | Database: PDB / ID: 1zta | ||||||
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| Title | THE SOLUTION STRUCTURE OF A LEUCINE-ZIPPER MOTIF PEPTIDE | ||||||
Components | LEUCINE ZIPPER MONOMER | ||||||
Keywords | DNA-BINDING MOTIF | ||||||
| Function / homology | Function and homology informationFCERI mediated MAPK activation / protein localization to nuclear periphery / Activation of the AP-1 family of transcription factors / response to amino acid starvation / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / mediator complex binding / Oxidative Stress Induced Senescence / TFIID-class transcription factor complex binding / amino acid biosynthetic process ...FCERI mediated MAPK activation / protein localization to nuclear periphery / Activation of the AP-1 family of transcription factors / response to amino acid starvation / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / mediator complex binding / Oxidative Stress Induced Senescence / TFIID-class transcription factor complex binding / amino acid biosynthetic process / positive regulation of RNA polymerase II transcription preinitiation complex assembly / positive regulation of transcription initiation by RNA polymerase II / cellular response to nutrient levels / cellular response to amino acid starvation / RNA polymerase II transcription regulator complex / DNA-binding transcription activator activity, RNA polymerase II-specific / transcription regulator complex / sequence-specific DNA binding / RNA polymerase II-specific DNA-binding transcription factor binding / DNA-binding transcription factor activity, RNA polymerase II-specific / intracellular signal transduction / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / chromatin binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / identical protein binding / nucleus Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR | ||||||
Authors | Saudek, V. / Pastore, A. / Castiglione Morelli, M.A. / Frank, R. / Gausepohl, H. / Gibson, T. | ||||||
Citation | Journal: Protein Eng. / Year: 1991Title: The solution structure of a leucine-zipper motif peptide. Authors: Saudek, V. / Pastore, A. / Morelli, M.A. / Frank, R. / Gausepohl, H. / Gibson, T. #1: Journal: Protein Eng. / Year: 1990Title: Solution Structure of the DNA-Binding Domain of the Yeast Transcriptional Activator Protein GCN4 Authors: Saudek, V. / Pastore, A. / Castiglione Morelli, M.A. / Frank, R. / Gausepohl, H. / Gibson, T. / Weih, F. / Roesch, P. #2: Journal: Biochemistry / Year: 1991Title: Solution Structure of the Basic Region from the Transcriptional Activator GCN4 Authors: Pastore, A. / Saudek, V. / Castiglione Morelli, M.A. / Frank, R. / Gausepohl, H. / Gibson, T. / Weih, F. / Roesch, P. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1zta.cif.gz | 152.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1zta.ent.gz | 96.2 KB | Display | PDB format |
| PDBx/mmJSON format | 1zta.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zt/1zta ftp://data.pdbj.org/pub/pdb/validation_reports/zt/1zta | HTTPS FTP |
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-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein/peptide | Mass: 4246.950 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: P03069 |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR |
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Sample preparation
| Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
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| NMR ensemble | Conformers submitted total number: 20 |
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