+Open data
-Basic information
Entry | Database: PDB / ID: 1bh2 | ||||||
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Title | A326S MUTANT OF AN INHIBITORY ALPHA SUBUNIT | ||||||
Components | GUANINE NUCLEOTIDE-BINDING PROTEIN | ||||||
Keywords | SIGNAL TRANSDUCTION PROTEIN | ||||||
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 / G alpha (i) signalling events / negative regulation of synaptic transmission / GTPase activating protein binding / positive regulation of protein localization to cell cortex / regulation of cAMP-mediated signaling / D2 dopamine receptor binding ...Extra-nuclear estrogen signaling / Adenylate cyclase inhibitory pathway / Adrenaline,noradrenaline inhibits insulin secretion / ADP signalling through P2Y purinoceptor 12 / G alpha (i) signalling events / negative regulation of synaptic transmission / GTPase activating protein binding / 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 / cell cycle / G protein-coupled receptor signaling pathway / cell division / GTPase activity / centrosome / 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 / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Mixon, M.B. / Posner, B.A. / Wall, M.A. / Gilman, A.G. / Sprang, S.R. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1998 Title: The A326S mutant of Gialpha1 as an approximation of the receptor-bound state. Authors: Posner, B.A. / Mixon, M.B. / Wall, M.A. / Sprang, S.R. / Gilman, A.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bh2.cif.gz | 75.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bh2.ent.gz | 58.7 KB | Display | PDB format |
PDBx/mmJSON format | 1bh2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bh/1bh2 ftp://data.pdbj.org/pub/pdb/validation_reports/bh/1bh2 | HTTPS FTP |
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-Related structure data
Related structure data | 1giaS S: Starting model for refinement |
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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: 36139.172 Da / Num. of mol.: 1 / Mutation: A326S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Cell line: BL21 / Organ: BRAIN / Plasmid: PQE6/GIA1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P10824 |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-GSP / |
#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: 2.4 Å3/Da / Density % sol: 49 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6 Details: PROTEIN WAS CRYSTALLIZED FROM 0.1M SODIUM ACETATE, PH 6.0, 2.0-2.1 M AMMONIUM SULFITE | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21 ℃ / Method: vapor diffusion, sitting drop / Details: Coleman, D.E., (1994) Science, 265, 1405. | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.918 |
Detector | Detector: CCD / Date: Dec 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→30 Å / Num. obs: 20438 / % possible obs: 88.4 % / Redundancy: 2.2 % / Rsym value: 0.066 / Net I/σ(I): 10.8 |
Reflection shell | Resolution: 2.1→2.15 Å / Mean I/σ(I) obs: 4.6 / Rsym value: 0.176 / % possible all: 88.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1GIA Resolution: 2.1→18 Å / Cross valid method: ALL BUT LAST ROUND / σ(F): 1
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Displacement parameters | Biso mean: 25.91 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→18 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 25.911 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 2.2 Å / Rfactor Rfree: 0.3 / Rfactor Rwork: 0.27 |