+Open data
-Basic information
Entry | Database: PDB / ID: 2i59 | ||||||
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Title | Solution structure of RGS10 | ||||||
Components | Regulator of G-protein signaling 10 | ||||||
Keywords | SIGNALING PROTEIN / Regulator of G-protein signaling / Structural Genomics / Structural Genomics Consortium / SGC | ||||||
Function / homology | Function and homology information regulation of G protein-coupled receptor signaling pathway / G-protein alpha-subunit binding / negative regulation of signal transduction / GTPase activator activity / G protein-coupled acetylcholine receptor signaling pathway / positive regulation of GTPase activity / G alpha (i) signalling events / nuclear body / G protein-coupled receptor signaling pathway / GTPase activity ...regulation of G protein-coupled receptor signaling pathway / G-protein alpha-subunit binding / negative regulation of signal transduction / GTPase activator activity / G protein-coupled acetylcholine receptor signaling pathway / positive regulation of GTPase activity / G alpha (i) signalling events / nuclear body / G protein-coupled receptor signaling pathway / GTPase activity / synapse / nucleoplasm / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Fedorov, O. / Higman, V.A. / Diehl, A. / Leidert, M. / Lemak, A. / Schmieder, P. / Oschkinat, H. / Elkins, J. / Soundarajan, M. / Doyle, D.A. ...Fedorov, O. / Higman, V.A. / Diehl, A. / Leidert, M. / Lemak, A. / Schmieder, P. / Oschkinat, H. / Elkins, J. / Soundarajan, M. / Doyle, D.A. / Arrowsmith, C. / Sundstrom, M. / Weigelt, J. / Edwards, A. / Ball, L.J. / Structural Genomics Consortium (SGC) | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2008 Title: Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. Authors: Soundararajan, M. / Willard, F.S. / Kimple, A.J. / Turnbull, A.P. / Ball, L.J. / Schoch, G.A. / Gileadi, C. / Fedorov, O.Y. / Dowler, E.F. / Higman, V.A. / Hutsell, S.Q. / Sundstrom, M. / ...Authors: Soundararajan, M. / Willard, F.S. / Kimple, A.J. / Turnbull, A.P. / Ball, L.J. / Schoch, G.A. / Gileadi, C. / Fedorov, O.Y. / Dowler, E.F. / Higman, V.A. / Hutsell, S.Q. / Sundstrom, M. / Doyle, D.A. / Siderovski, D.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2i59.cif.gz | 892.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2i59.ent.gz | 750.5 KB | Display | PDB format |
PDBx/mmJSON format | 2i59.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i5/2i59 ftp://data.pdbj.org/pub/pdb/validation_reports/i5/2i59 | HTTPS FTP |
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-Related structure data
Related structure data | 1zv4C 2a72C 2af0C 2bt2C 2bv1C 2es0C 2gtpC 2ihbC 2ihdC 2ik8C 2jm5C 2jnuC 2odeC 2owiC C: citing same article (ref.) |
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Similar structure data | |
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: 16510.805 Da / Num. of mol.: 1 / Fragment: Regulator of G-protein signaling domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RGS10 / Production host: Escherichia coli (E. coli) / References: UniProt: O43665 |
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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: U-15N, 13C RGS10, 20 mM Phosphate, 50 mM NaCl, 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 50 mM NaCl, 20 mM phosphate / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |