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Yorodumi- PDB-1gcn: X-RAY ANALYSIS OF GLUCAGON AND ITS RELATIONSHIP TO RECEPTOR BINDING -
+Open data
-Basic information
Entry | Database: PDB / ID: 1gcn | ||||||
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Title | X-RAY ANALYSIS OF GLUCAGON AND ITS RELATIONSHIP TO RECEPTOR BINDING | ||||||
Components | GLUCAGON | ||||||
Keywords | HORMONE | ||||||
Function / homology | Function and homology information Glucagon signaling in metabolic regulation / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / G alpha (s) signalling events / Glucagon-type ligand receptors / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / G alpha (q) signalling events / Synthesis, secretion, and deacylation of Ghrelin / glucagon receptor binding / negative regulation of execution phase of apoptosis / : ...Glucagon signaling in metabolic regulation / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / G alpha (s) signalling events / Glucagon-type ligand receptors / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / G alpha (q) signalling events / Synthesis, secretion, and deacylation of Ghrelin / glucagon receptor binding / negative regulation of execution phase of apoptosis / : / cellular response to glucagon stimulus / positive regulation of calcium ion import / positive regulation of insulin secretion involved in cellular response to glucose stimulus / regulation of insulin secretion / protein kinase A signaling / positive regulation of gluconeogenesis / response to activity / positive regulation of peptidyl-threonine phosphorylation / gluconeogenesis / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / hormone activity / glucose homeostasis / positive regulation of peptidyl-serine phosphorylation / positive regulation of ERK1 and ERK2 cascade / negative regulation of apoptotic process / extracellular space / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Sus scrofa (pig) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3 Å | ||||||
Authors | Blundell, T.L. / Sasaki, K. / Dockerill, S. / Tickle, I.J. | ||||||
Citation | Journal: Nature / Year: 1975 Title: X-ray analysis of glucagon and its relationship to receptor binding. Authors: Sasaki, K. / Dockerill, S. / Adamiak, D.A. / Tickle, I.J. / Blundell, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gcn.cif.gz | 14.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gcn.ent.gz | 8.8 KB | Display | PDB format |
PDBx/mmJSON format | 1gcn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gc/1gcn ftp://data.pdbj.org/pub/pdb/validation_reports/gc/1gcn | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES 1 THROUGH 5 ARE RATHER DISORDERED IN THE CRYSTALS. |
-Components
#1: Protein/peptide | Mass: 3486.781 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / References: UniProt: P01274 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.74 % | |||||||||||||||
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Crystal grow | *PLUS Temperature: 50 ℃ / pH: 9.2 / Method: unknown | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Refinement | Highest resolution: 3 Å | ||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 3 Å
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