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Open data
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Basic information
Entry | Database: PDB / ID: 1ezy | ||||||
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Title | HIGH-RESOLUTION SOLUTION STRUCTURE OF FREE RGS4 BY NMR | ||||||
![]() | REGULATOR OF G-PROTEIN SIGNALING 4 | ||||||
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Function / homology | ![]() negative regulation of glycine import across plasma membrane / negative regulation of dopamine receptor signaling pathway / negative regulation of potassium ion transmembrane transport / dorsal root ganglion development / negative regulation of G protein-coupled receptor signaling pathway / negative regulation of cell growth involved in cardiac muscle cell development / regulation of actin filament organization / G alpha (q) signalling events / positive regulation of heart rate / G alpha (i) signalling events ...negative regulation of glycine import across plasma membrane / negative regulation of dopamine receptor signaling pathway / negative regulation of potassium ion transmembrane transport / dorsal root ganglion development / negative regulation of G protein-coupled receptor signaling pathway / negative regulation of cell growth involved in cardiac muscle cell development / regulation of actin filament organization / G alpha (q) signalling events / positive regulation of heart rate / G alpha (i) signalling events / regulation of potassium ion transmembrane transport / response to morphine / G-protein alpha-subunit binding / regulation of calcium ion transport / response to cocaine / positive regulation of excitatory postsynaptic potential / response to amphetamine / ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Moy, F.J. / Chanda, P.K. / Cockett, M.I. / Edris, W. / Jones, P.G. / Mason, K. / Semus, S. / Powers, R. | ||||||
![]() | ![]() Title: NMR structure of free RGS4 reveals an induced conformational change upon binding Galpha. Authors: Moy, F.J. / Chanda, P.K. / Cockett, M.I. / Edris, W. / Jones, P.G. / Mason, K. / Semus, S. / Powers, R. #1: ![]() Title: 1H, 15N, 13C and 13CO Assignments and Secondary Structure Determination of RGS4 Authors: Moy, F.J. / Chanda, P.K. / Cockett, M.I. / Edris, W. / Jones, P.G. / Powers, R. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.2 MB | Display | ![]() |
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PDB format | ![]() | 1.1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 350.1 KB | Display | ![]() |
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Full document | ![]() | 576.2 KB | Display | |
Data in XML | ![]() | 80.4 KB | Display | |
Data in CIF | ![]() | 104.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 19145.711 Da / Num. of mol.: 1 / Fragment: CORE DOMAIN OF RGS Source method: isolated from a genetically manipulated source Details: SIX RESIDUE HISTIDINE TAG AT C-TERMINUS / Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
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NMR experiment |
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Sample preparation
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Crystal grow![]() | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model![]() |
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Processing
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Refinement | Method: distance geometry simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 2871 restraints, 3167 are NOE-derived distance constraints, 431 dihedral angle restraints,78 distance restraints from 39 backbone hydrogen bond, 132 ...Details: the structures are based on a total of 2871 restraints, 3167 are NOE-derived distance constraints, 431 dihedral angle restraints,78 distance restraints from 39 backbone hydrogen bond, 132 3JHNa restraints, 136 Ca and 134 Cb chemical shift restraints and the use of a conformational database target function. | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy,target function Conformers calculated total number: 100 / Conformers submitted total number: 30 |