+Open data
-Basic information
Entry | Database: PDB / ID: 2af0 | ||||||
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Title | Structure of the Regulator of G-Protein Signaling Domain of RGS2 | ||||||
Components | Regulator of G-protein signaling 2 | ||||||
Keywords | SIGNALING PROTEIN / HELIX / Structural Genomics / Structural Genomics Consortium / SGC | ||||||
Function / homology | Function and homology information regulation of adenylate cyclase-inhibiting adrenergic receptor signaling pathway / negative regulation of phospholipase activity / negative regulation of glycine import across plasma membrane / adenylate cyclase inhibitor activity / negative regulation of cardiac muscle hypertrophy / negative regulation of cell growth involved in cardiac muscle cell development / negative regulation of G protein-coupled receptor signaling pathway / regulation of G protein-coupled receptor signaling pathway / relaxation of vascular associated smooth muscle / relaxation of cardiac muscle ...regulation of adenylate cyclase-inhibiting adrenergic receptor signaling pathway / negative regulation of phospholipase activity / negative regulation of glycine import across plasma membrane / adenylate cyclase inhibitor activity / negative regulation of cardiac muscle hypertrophy / negative regulation of cell growth involved in cardiac muscle cell development / negative regulation of G protein-coupled receptor signaling pathway / regulation of G protein-coupled receptor signaling pathway / relaxation of vascular associated smooth muscle / relaxation of cardiac muscle / beta-tubulin binding / G-protein alpha-subunit binding / maternal process involved in female pregnancy / brown fat cell differentiation / positive regulation of cardiac muscle contraction / response to amphetamine / GTPase activator activity / negative regulation of MAP kinase activity / cytoplasmic side of plasma membrane / positive regulation of neuron projection development / G alpha (q) signalling events / spermatogenesis / response to ethanol / negative regulation of translation / calmodulin binding / cell cycle / G protein-coupled receptor signaling pathway / GTPase activity / nucleolus / mitochondrion / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Papagrigoriou, E. / Johannson, C. / Phillips, C. / Smee, C. / Elkins, J.M. / Weigelt, J. / Arrowsmith, C. / Edwards, A. / Sundstrom, M. / Von Delft, F. ...Papagrigoriou, E. / Johannson, C. / Phillips, C. / Smee, C. / Elkins, J.M. / Weigelt, J. / Arrowsmith, C. / Edwards, A. / Sundstrom, M. / Von Delft, F. / Doyle, D.A. / 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 | 2af0.cif.gz | 40.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2af0.ent.gz | 28.1 KB | Display | PDB format |
PDBx/mmJSON format | 2af0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/af/2af0 ftp://data.pdbj.org/pub/pdb/validation_reports/af/2af0 | HTTPS FTP |
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-Related structure data
Related structure data | 1zv4C 2a72C 2bt2C 2bv1C 2es0C 2gtpC 2i59C 2ihbC 2ihdC 2ik8C 2jm5C 2jnuC 2odeC 2owiC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 16994.148 Da / Num. of mol.: 1 / Fragment: residues 71-203 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P41220 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 37.9 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: (NH4)2SO4, NaCl, cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9773 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 10, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9773 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→36.9 Å / Num. all: 7531 / Num. obs: 7422 / % possible obs: 98.6 % |
Reflection shell | Resolution: 2.3→2.38 Å / % possible all: 99.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.3→33.69 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.946 / SU B: 22.428 / SU ML: 0.233 / Cross valid method: THROUGHOUT / ESU R: 0.394 / ESU R Free: 0.251 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 55.407 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→33.69 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.359 Å / Total num. of bins used: 20
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