+Open data
-Basic information
Entry | Database: PDB / ID: 1git | ||||||
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Title | STRUCTURE OF GTP-BINDING PROTEIN | ||||||
Components | G PROTEIN GI ALPHA 1 | ||||||
Keywords | GTP-BINDING PROTEIN / GTP-ASE / TRANSDUCER / ADENYLATE CYCLASE / MULTIGENE FAMILY / MYRISTYLATION | ||||||
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 / Resolution: 2.6 Å | ||||||
Authors | Berghuis, A.M. / Lee, E. / Sprang, S.R. | ||||||
Citation | Journal: Structure / Year: 1996 Title: Structure of the GDP-Pi complex of Gly203-->Ala gialpha1: a mimic of the ternary product complex of galpha-catalyzed GTP hydrolysis. Authors: Berghuis, A.M. / Lee, E. / Raw, A.S. / Gilman, A.G. / Sprang, S.R. #1: Journal: Science / Year: 1995 Title: Tertiary and Quaternary Structural Changes in Gi Alpha 1 Induced by GTP Hydrolysis Authors: Mixon, M.B. / Lee, E. / Coleman, D.E. / Berghuis, A.M. / Gilman, A.G. / Sprang, S.R. #2: 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. #3: 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1git.cif.gz | 77.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1git.ent.gz | 57.8 KB | Display | PDB format |
PDBx/mmJSON format | 1git.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gi/1git ftp://data.pdbj.org/pub/pdb/validation_reports/gi/1git | HTTPS FTP |
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-Related structure data
Similar structure data |
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-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: G203A Source method: isolated from a genetically manipulated source Details: STRUCTURE MIMICS THE TERNARY COMPLEX / Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: PQE6 VECTOR / Production host: Escherichia coli (E. coli) / References: UniProt: P10824 |
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#2: Chemical | ChemComp-PO4 / |
#3: Chemical | ChemComp-GDP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.67 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 8 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F2 / Wavelength: 0.979 |
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Detector | Type: FUJI / Detector: IMAGE PLATE / Date: 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Num. obs: 11856 / % possible obs: 84.1 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Rmerge(I) obs: 0.04 |
Reflection | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 40 Å / Num. measured all: 28864 / Rmerge(I) obs: 0.03 |
Reflection shell | *PLUS % possible obs: 86.5 % / Rmerge(I) obs: 0.09 |
-Processing
Software |
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Refinement | Resolution: 2.6→8 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 1
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.6→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.71 Å / Total num. of bins used: 8
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.231 |