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Open data
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Basic information
| Entry | Database: PDB / ID: 1dep | ||||||
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| Title | MEMBRANE PROTEIN, NMR, 1 STRUCTURE | ||||||
Components | T345-359 | ||||||
Keywords | MEMBRANE PROTEIN / BETA-ADRENOCEPTOR / MICELLE-BOUND PEPTIDE | ||||||
| Function / homology | Function and homology informationbeta1-adrenergic receptor activity / positive regulation of heart contraction / regulation of circadian sleep/wake cycle, sleep / norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure / adenylate cyclase-activating adrenergic receptor signaling pathway / early endosome / positive regulation of MAPK cascade / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR | ||||||
Authors | Jung, H. / Schnackerz, K.D. | ||||||
Citation | Journal: FEBS Lett. / Year: 1995Title: NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor. Authors: Jung, H. / Windhaber, R. / Palm, D. / Schnackerz, K.D. #1: Journal: Eur.J.Biochem. / Year: 1991Title: Multisite Contacts Involved in Coupling of the Beta-Adrenergic Receptor with the Stimulatory Guanine-Nucleotide-Binding Regulatory Protein. Structural and Functional Studies by Beta-Receptor- ...Title: Multisite Contacts Involved in Coupling of the Beta-Adrenergic Receptor with the Stimulatory Guanine-Nucleotide-Binding Regulatory Protein. Structural and Functional Studies by Beta-Receptor-Site-Specific Synthetic Peptides Authors: Munch, G. / Dees, C. / Hekman, M. / Palm, D. | ||||||
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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 | 1dep.cif.gz | 12.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1dep.ent.gz | 7.3 KB | Display | PDB format |
| PDBx/mmJSON format | 1dep.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1dep_validation.pdf.gz | 237 KB | Display | wwPDB validaton report |
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| Full document | 1dep_full_validation.pdf.gz | 236.7 KB | Display | |
| Data in XML | 1dep_validation.xml.gz | 1.7 KB | Display | |
| Data in CIF | 1dep_validation.cif.gz | 1.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/de/1dep ftp://data.pdbj.org/pub/pdb/validation_reports/de/1dep | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| NMR ensembles |
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Components
| #1: Protein/peptide | Mass: 1889.294 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: THE PEPTIDE T345-359 REPRESENTS THE FOURTH INTRACELLULAR LOOP OF THE BETA-ADRENOCEPTOR FROM TURKEY Source: (gene. exp.) ![]() |
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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
| NMR software | Name: EREF / Developer: JACK,LEVITT / Classification: refinement |
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| NMR ensemble | Conformers submitted total number: 1 |
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