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Open data
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Basic information
Entry | Database: PDB / ID: 2a72 | ||||||
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Title | Structure of the regulator of G-protein signaling domain of RGS7 | ||||||
![]() | Regulator of G-protein signalling 7 | ||||||
![]() | SIGNALING PROTEIN / Human RGS7 / regulator of G-protein signaling 7 / GTPase-activating proteins (GAP) / Structural Genomics / Structural Genomics Consortium / SGC | ||||||
Function / homology | ![]() negative regulation of G protein-coupled receptor signaling pathway / positive regulation of potassium ion transmembrane transport / regulation of G protein-coupled receptor signaling pathway / G-protein alpha-subunit binding / response to amphetamine / GTPase activator activity / positive regulation of GTPase activity / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / G-protein beta-subunit binding / nuclear envelope ...negative regulation of G protein-coupled receptor signaling pathway / positive regulation of potassium ion transmembrane transport / regulation of G protein-coupled receptor signaling pathway / G-protein alpha-subunit binding / response to amphetamine / GTPase activator activity / positive regulation of GTPase activity / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / G-protein beta-subunit binding / nuclear envelope / G alpha (i) signalling events / response to ethanol / intracellular signal transduction / neuron projection / G protein-coupled receptor signaling pathway / GTPase activity / protein-containing complex / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Schoch, G.A. / Johansson, C. / Phillips, C. / Debreczeni, J. / Smee, C. / Elkins, J.M. / Sundstrom, M. / Edwards, A. / Arrowsmith, C. / von Delft, F. ...Schoch, G.A. / Johansson, C. / Phillips, C. / Debreczeni, J. / Smee, C. / Elkins, J.M. / Sundstrom, M. / Edwards, A. / Arrowsmith, C. / von Delft, F. / Gileadi, O. / Doyle, D.A. / Structural Genomics Consortium (SGC) | ||||||
![]() | ![]() 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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Remark 300 | BIOMOLECULE: Two biological units are present in the asymmetric unit that are formed from the ...BIOMOLECULE: Two biological units are present in the asymmetric unit that are formed from the combinations of residues 320 to 414 of chain A with 415 to 450 of chain B and residues 320 to 414 of chain B with 415 to 450 of chain A. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 72.2 KB | Display | ![]() |
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PDB format | ![]() | 54.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 430.3 KB | Display | ![]() |
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Full document | ![]() | 431.2 KB | Display | |
Data in XML | ![]() | 14.1 KB | Display | |
Data in CIF | ![]() | 20 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1zv4C ![]() 2af0C ![]() 2bt2C ![]() 2bv1C ![]() 2es0C ![]() 2gtpC ![]() 2i59C ![]() 2ihbC ![]() 2ihdC ![]() 2ik8C ![]() 2jm5C ![]() 2jnuC ![]() 2odeC ![]() 2owiC 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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: ARG / Beg label comp-ID: ARG / End auth comp-ID: ALA / End label comp-ID: ALA / Refine code: 5 / Auth seq-ID: 326 - 443 / Label seq-ID: 9 - 126
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Components
#1: Protein | Mass: 17138.375 Da / Num. of mol.: 2 / Fragment: RESIDUES 320-463 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-CL / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41.1 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: PEG 3350, (NH4)2SO4, BIS-TRIS, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS HTC / Detector: IMAGE PLATE / Date: Jun 13, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→45.93 Å / Num. all: 19896 / Num. obs: 19896 / % possible obs: 95.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Biso Wilson estimate: 28.3 Å2 / Rmerge(I) obs: 0.068 / Rsym value: 0.079 / Net I/σ(I): 14.9 |
Reflection shell | Resolution: 2→2.11 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.434 / Mean I/σ(I) obs: 2.2 / Num. unique all: 2457 / Rsym value: 0.536 / % possible all: 81.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1FQJ_B.pdb Resolution: 2→53 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.911 / SU B: 9.269 / SU ML: 0.136 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.195 / ESU R Free: 0.184 / 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: 28.8 Å2
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Refinement step | Cycle: LAST / Resolution: 2→53 Å
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Refine LS restraints |
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Refine LS restraints NCS | Dom-ID: 1 / Auth asym-ID: A / Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 2→2.052 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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