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- PDB-5ott: Extracellular domain of GLP-1 receptor in complex with exendin-4 ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5ott | ||||||
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Title | Extracellular domain of GLP-1 receptor in complex with exendin-4 variant Gly2Hcs/Thr5Hcs | ||||||
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![]() | SIGNALING PROTEIN / glucagon-like peptide 1 / GPCR / cyclic peptides | ||||||
Function / homology | ![]() glucagon-like peptide 1 receptor activity / glucagon receptor activity / hormone secretion / positive regulation of blood pressure / post-translational protein targeting to membrane, translocation / response to psychosocial stress / regulation of heart contraction / peptide hormone binding / activation of adenylate cyclase activity / negative regulation of blood pressure ...glucagon-like peptide 1 receptor activity / glucagon receptor activity / hormone secretion / positive regulation of blood pressure / post-translational protein targeting to membrane, translocation / response to psychosocial stress / regulation of heart contraction / peptide hormone binding / activation of adenylate cyclase activity / negative regulation of blood pressure / cAMP-mediated signaling / regulation of blood pressure / adenylate cyclase-activating G protein-coupled receptor signaling pathway / hormone activity / transmembrane signaling receptor activity / Glucagon-type ligand receptors / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / positive regulation of cytosolic calcium ion concentration / G alpha (s) signalling events / toxin activity / learning or memory / cell surface receptor signaling pathway / extracellular region / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Mortensen, S. | ||||||
![]() | ![]() Title: alpha-Helix or beta-Turn? An Investigation into N-Terminally Constrained Analogues of Glucagon-like Peptide 1 (GLP-1) and Exendin-4. Authors: Oddo, A. / Mortensen, S. / Thogersen, H. / De Maria, L. / Hennen, S. / McGuire, J.N. / Kofoed, J. / Linderoth, L. / Reedtz-Runge, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 45.4 KB | Display | ![]() |
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PDB format | ![]() | 30.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5otuC ![]() 5otvC ![]() 5otwC ![]() 5otxC ![]() 4zgmS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 13547.892 Da / Num. of mol.: 1 / Fragment: extracellular domain, UNP residues 24-139 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 4267.772 Da / Num. of mol.: 1 / Mutation: G2HCS, T5HCS / Source method: obtained synthetically / Source: (synth.) ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.53 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 0.1 M Imidazole pH 6.5, 1.0 M Sodium acetate trihydrate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: DECTRIS PILATUS3 R 1M / Detector: PIXEL / Date: Feb 24, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54187 Å / Relative weight: 1 |
Reflection | Resolution: 1.92→47.382 Å / Num. obs: 15019 / % possible obs: 99 % / Redundancy: 12.9 % / CC1/2: 0.999 / Rmerge(I) obs: 0.103 / Rpim(I) all: 0.03 / Rsym value: 0.108 / Net I/σ(I): 19.8 |
Reflection shell | Resolution: 1.92→1.95 Å / Redundancy: 12.66 % / Rmerge(I) obs: 1.145 / Mean I/σ(I) obs: 2.3 / Num. measured obs: 9519 / Num. unique all: 752 / Rpim(I) all: 0.33 / Rrim(I) all: 1.193 / % possible all: 97.41 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4ZGM Resolution: 1.92→47.382 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 21.35
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.92→47.382 Å
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Refine LS restraints |
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LS refinement shell |
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