+Open data
-Basic information
Entry | Database: PDB / ID: 1as3 | ||||||
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Title | GDP BOUND G42V GIA1 | ||||||
Components | GIA1 | ||||||
Keywords | SIGNAL TRANSDUCTION / GTPASE | ||||||
Function / homology | Function and homology information Extra-nuclear estrogen signaling / Adenylate cyclase inhibitory pathway / Adrenaline,noradrenaline inhibits insulin secretion / ADP signalling through P2Y purinoceptor 12 / GTPase activating protein binding / negative regulation of synaptic transmission / G alpha (i) signalling events / neurotransmitter receptor localization to postsynaptic specialization membrane / positive regulation of protein localization to cell cortex / regulation of cAMP-mediated signaling ...Extra-nuclear estrogen signaling / Adenylate cyclase inhibitory pathway / Adrenaline,noradrenaline inhibits insulin secretion / ADP signalling through P2Y purinoceptor 12 / GTPase activating protein binding / negative regulation of synaptic transmission / G alpha (i) signalling events / neurotransmitter receptor localization to postsynaptic specialization membrane / positive regulation of protein localization to cell cortex / regulation of cAMP-mediated signaling / D2 dopamine receptor binding / G protein-coupled serotonin receptor binding / regulation of mitotic spindle organization / cellular response to forskolin / G protein-coupled receptor binding / G-protein beta/gamma-subunit complex binding / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / GDP binding / heterotrimeric G-protein complex / cell cortex / midbody / postsynapse / G protein-coupled receptor signaling pathway / cell division / GTPase activity / centrosome / glutamatergic synapse / GTP binding / magnesium ion binding / protein-containing complex / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / DIFFERENCE FOURIER / Resolution: 2.4 Å | ||||||
Authors | Raw, A.S. / Coleman, D.E. / Gilman, A.G. / Sprang, S.R. | ||||||
Citation | Journal: Biochemistry / Year: 1997 Title: Structural and biochemical characterization of the GTPgammaS-, GDP.Pi-, and GDP-bound forms of a GTPase-deficient Gly42 --> Val mutant of Gialpha1. Authors: Raw, A.S. / Coleman, D.E. / Gilman, A.G. / Sprang, S.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1as3.cif.gz | 80.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1as3.ent.gz | 59.6 KB | Display | PDB format |
PDBx/mmJSON format | 1as3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1as3_validation.pdf.gz | 748.3 KB | Display | wwPDB validaton report |
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Full document | 1as3_full_validation.pdf.gz | 752.2 KB | Display | |
Data in XML | 1as3_validation.xml.gz | 14.9 KB | Display | |
Data in CIF | 1as3_validation.cif.gz | 20.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/1as3 ftp://data.pdbj.org/pub/pdb/validation_reports/as/1as3 | HTTPS FTP |
-Related structure data
Related structure data | 1as0C 1as2C 1gddS S: Starting model for refinement 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: 40309.914 Da / Num. of mol.: 1 / Mutation: G42V Source method: isolated from a genetically manipulated source Details: GDP BOUND G42V GIA1 / Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: PQE-6 / Species (production host): Escherichia coli / Cell line (production host): BL21 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P10824 |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-GDP / |
#4: 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: 3.12 Å3/Da / Density % sol: 60.61 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 8 Details: THE PROTEIN WAS CRYSTALLIZED IN HANGING DROPS USING 4M (NH4)2SO3 AS THE PRECIPITANT. 50 MM HEPES, PH 8.0, 10 MM MGSO4, 10 MM DTT AND 5 MM GDP WAS THE BUFFER., vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.918 |
Detector | Detector: CCD / Date: Sep 1, 1996 / Details: MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→15 Å / Num. obs: 19384 / % possible obs: 99.3 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.063 / Net I/σ(I): 20.5 |
Reflection shell | Resolution: 2.4→2.49 Å / Rmerge(I) obs: 0.33 / % possible all: 99.2 |
-Processing
Software |
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: PDB ENTRY 1GDD Resolution: 2.4→8 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 1
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Displacement parameters | Biso mean: 42.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.51 Å / Total num. of bins used: 8
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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