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Yorodumi- PDB-1gfi: STRUCTURES OF ACTIVE CONFORMATIONS OF GI ALPHA 1 AND THE MECHANIS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1gfi | ||||||
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Title | STRUCTURES OF ACTIVE CONFORMATIONS OF GI ALPHA 1 AND THE MECHANISM OF GTP HYDROLYSIS | ||||||
Components | GUANINE NUCLEOTIDE-BINDING PROTEIN G | ||||||
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 / Resolution: 2.2 Å | ||||||
Authors | Coleman, D.E. / Berghuis, A.M. / Sprang, S.R. | ||||||
Citation | Journal: Science / Year: 1994 Title: Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. Authors: Coleman, D.E. / Berghuis, A.M. / Lee, E. / Linder, M.E. / Gilman, A.G. / Sprang, S.R. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Crystallization and Preliminary Crystallographic Studies of GI Alpha 1 and Mutants of GI Alpha 1 in the GTP and Gdp-Bound States Authors: Coleman, D.E. / Lee, E. / Mixon, M.B. / Linder, M.E. / Berghuis, A.M. / 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 | 1gfi.cif.gz | 78.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gfi.ent.gz | 58.1 KB | Display | PDB format |
PDBx/mmJSON format | 1gfi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gf/1gfi ftp://data.pdbj.org/pub/pdb/validation_reports/gf/1gfi | HTTPS FTP |
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-Related 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: 40267.836 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: PQE6 VECTOR / References: UniProt: P10824 |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-ALF / |
#4: Chemical | ChemComp-GDP / |
#5: Water | ChemComp-HOH / |
Nonpolymer details | COMPND GDP-ALF4 IS A TRANSITION |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.3 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 21 ℃ / pH: 6 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Radiation | Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 19715 / % possible obs: 97.8 % |
Reflection | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 15 Å / Num. measured all: 96580 / Rmerge(I) obs: 0.053 |
-Processing
Software |
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Refinement | Resolution: 2.2→8 Å / σ(F): 1
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Displacement parameters | Biso mean: 20.2 Å2 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refinement | *PLUS Num. reflection obs: 17407 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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