+Open data
-Basic information
Entry | Database: PDB / ID: 1ezt | ||||||
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Title | HIGH-RESOLUTION SOLUTION STRUCTURE OF FREE RGS4 BY NMR | ||||||
Components | REGULATOR OF G-PROTEIN SIGNALING 4 | ||||||
Keywords | SIGNALING PROTEIN INHIBITOR / 4-helix-bundle / free form of protein | ||||||
Function / homology | Function and homology information 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 cell growth involved in cardiac muscle cell development / regulation of actin filament organization / regulation of potassium ion transmembrane transport / G alpha (q) signalling events / G alpha (i) signalling events / negative regulation of G protein-coupled receptor signaling pathway ...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 cell growth involved in cardiac muscle cell development / regulation of actin filament organization / regulation of potassium ion transmembrane transport / G alpha (q) signalling events / G alpha (i) signalling events / negative regulation of G protein-coupled receptor signaling pathway / positive regulation of heart rate / regulation of calcium ion transport / positive regulation of excitatory postsynaptic potential / G-protein alpha-subunit binding / response to amphetamine / GTPase activator activity / response to cocaine / response to ethanol / protein kinase binding / protein-containing complex / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing | ||||||
Authors | Moy, F.J. / Chanda, P.K. / Cockett, M.I. / Edris, W. / Jones, P.G. / Mason, K. / Semus, S. / Powers, R. | ||||||
Citation | Journal: Biochemistry / Year: 2000 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: Journal: J.Biomol.NMR / Year: 1999 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ezt.cif.gz | 57.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ezt.ent.gz | 42.5 KB | Display | PDB format |
PDBx/mmJSON format | 1ezt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ezt_validation.pdf.gz | 247.8 KB | Display | wwPDB validaton report |
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Full document | 1ezt_full_validation.pdf.gz | 247.6 KB | Display | |
Data in XML | 1ezt_validation.xml.gz | 4 KB | Display | |
Data in CIF | 1ezt_validation.cif.gz | 5.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ez/1ezt ftp://data.pdbj.org/pub/pdb/validation_reports/ez/1ezt | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 19145.711 Da / Num. of mol.: 1 / Fragment: CORE RGS DOMAIN Source method: isolated from a genetically manipulated source Details: SIX RESIDUE HISTIDINE TAG AT C-TERMINUS / Source: (gene. exp.) Rattus norvegicus (Norway rat) / Organ: BRAIN / Plasmid: PRGS4 / Production host: Escherichia coli (E. coli) / References: UniProt: P49799 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 50 mM K / pH: 6 / Pressure: ambient / Temperature: 303 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: distance geometry simulated annealing / Software ordinal: 1 Details: The structure is based on a total of 2871 restraints, 1960 approximate interproton distance restraints, 78 distance restraints for 39 backbone hydrogen bonds, 431 torsion angle restraints, ...Details: The structure is based on a total of 2871 restraints, 1960 approximate interproton distance restraints, 78 distance restraints for 39 backbone hydrogen bonds, 431 torsion angle restraints, 132 3JHNa restraints, 136 Ca and 134 Cb chemical shift restraints. Structure also refined with conformational database target function. | ||||||||||||||||||||||||
NMR ensemble | Conformers submitted total number: 1 |