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Yorodumi- PDB-1gg2: G PROTEIN HETEROTRIMER MUTANT GI_ALPHA_1(G203A) BETA_1 GAMMA_2 WI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1gg2 | ||||||
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Title | G PROTEIN HETEROTRIMER MUTANT GI_ALPHA_1(G203A) BETA_1 GAMMA_2 WITH GDP BOUND | ||||||
Components |
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Keywords | COMPLEX (GTP-BINDING/TRANSDUCER) / SIGNAL TRANSDUCTION PROTEIN / G PROTEIN / WD40 / GTPASE / RAS / PROPELLER / COMPLEX (GTP-BINDING-TRANSDUCER) / COMPLEX (GTP-BINDING-TRANSDUCER) complex | ||||||
Function / homology | Function and homology information Extra-nuclear estrogen signaling / Adenylate cyclase inhibitory pathway / Olfactory Signaling Pathway / Sensory perception of sweet, bitter, and umami (glutamate) taste / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / Activation of the phototransduction cascade / Adrenaline,noradrenaline inhibits insulin secretion / ADP signalling through P2Y purinoceptor 12 / G alpha (i) signalling events / negative regulation of synaptic transmission ...Extra-nuclear estrogen signaling / Adenylate cyclase inhibitory pathway / Olfactory Signaling Pathway / Sensory perception of sweet, bitter, and umami (glutamate) taste / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / Activation of the phototransduction cascade / Adrenaline,noradrenaline inhibits insulin secretion / ADP signalling through P2Y purinoceptor 12 / G alpha (i) signalling events / negative regulation of synaptic transmission / Activation of G protein gated Potassium channels / G-protein activation / G beta:gamma signalling through PI3Kgamma / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through PLC beta / ADP signalling through P2Y purinoceptor 1 / Thromboxane signalling through TP receptor / Presynaptic function of Kainate receptors / G beta:gamma signalling through CDC42 / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / Glucagon-type ligand receptors / Adrenaline,noradrenaline inhibits insulin secretion / G alpha (12/13) signalling events / G beta:gamma signalling through BTK / ADP signalling through P2Y purinoceptor 12 / GTPase activating protein binding / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / Thrombin signalling through proteinase activated receptors (PARs) / Ca2+ pathway / G alpha (z) signalling events / Extra-nuclear estrogen signaling / G alpha (s) signalling events / G alpha (q) signalling events / G alpha (i) signalling events / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / Vasopressin regulates renal water homeostasis via Aquaporins / 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 / photoreceptor disc membrane / cellular response to catecholamine stimulus / adenylate cyclase-activating dopamine receptor signaling pathway / cellular response to prostaglandin E stimulus / sensory perception of taste / GDP binding / G-protein beta-subunit binding / heterotrimeric G-protein complex / signaling receptor complex adaptor activity / retina development in camera-type eye / GTPase binding / phospholipase C-activating G protein-coupled receptor signaling pathway / cell cortex / midbody / cell population proliferation / cell cycle / G protein-coupled receptor signaling pathway / cell division / GTPase activity / centrosome / protein-containing complex binding / GTP binding / magnesium ion binding / protein-containing complex / membrane / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / REFINEMENT WITH WILD-TYPE MODEL (SAME CELL) / Resolution: 2.4 Å | ||||||
Authors | Wall, M.A. / Sprang, S.R. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1995 Title: The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2. Authors: Wall, M.A. / Coleman, D.E. / Lee, E. / Iniguez-Lluhi, J.A. / Posner, B.A. / 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 | 1gg2.cif.gz | 166.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gg2.ent.gz | 130.1 KB | Display | PDB format |
PDBx/mmJSON format | 1gg2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gg/1gg2 ftp://data.pdbj.org/pub/pdb/validation_reports/gg/1gg2 | 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: 40281.863 Da / Num. of mol.: 1 / Fragment: ALPHA 1 / Mutation: CHAIN A, G203A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Cell line: SF9 / Production host: Escherichia coli (E. coli) / Strain (production host): SF9 / References: UniProt: P10824 |
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#2: Protein | Mass: 37416.930 Da / Num. of mol.: 1 / Fragment: BETA 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Cell line: SF9 / References: UniProt: P62871 |
#3: Protein | Mass: 7845.078 Da / Num. of mol.: 1 / Fragment: GAMMA 2 / Mutation: CHAIN G, C68S Source method: isolated from a genetically manipulated source Details: HETEROTRIMER MUTANT WITH BOUND GDP / Source: (gene. exp.) Bos taurus (cattle) Description: BOVINE BETA 1 AND GAMMA 2 WERE COEXPRESSED IN SF9 CELLS INFECTED WITH RECOMBINANT BACULOVIRUSES AND PURIFIED AS A COMPLEX Cell line: SF9 / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): SF9 / References: UniProt: P63212 |
#4: Chemical | ChemComp-GDP / |
#5: 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: 2.69 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 / Details: pH 7.0 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
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: 0.92 |
Detector | Detector: CCD / Date: Jan 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→25 Å / Num. obs: 32774 / % possible obs: 93 % / Observed criterion σ(I): -3 / Redundancy: 2.55 % / Rmerge(I) obs: 0.073 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 2.4→2.49 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.301 / Mean I/σ(I) obs: 2.28 / % possible all: 91 |
-Processing
Software |
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Refinement | Method to determine structure: REFINEMENT WITH WILD-TYPE MODEL (SAME CELL) Resolution: 2.4→15 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 100000 / Data cutoff low absF: 1.0E-5 / Cross valid method: THROUGHOUT / σ(F): 1 Details: AN OCCUPANCY OF 0.0 INDICATES THAT NO SIGNIFICANT ELECTRON DENSITY WAS FOUND IN THE FINAL FOURIER MAP.
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Displacement parameters | Biso mean: 61.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.36 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→15 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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