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- PDB-1gil: STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GT... -
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Basic information
Entry | Database: PDB / ID: 1gil | ||||||
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Title | STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS | ||||||
![]() | G PROTEIN GI ALPHA 1 | ||||||
![]() | GTP-BINDING PROTEIN | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Coleman, D.E. / Berghuis, A.M. / Sprang, S.R. | ||||||
![]() | ![]() 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: ![]() Title: Crystallization and Preliminary Crystallographic Studies of Gia1 and Mutants of Gia1 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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Remark 650 | HELIX HELIX HELIX_ID: AA,DISTORTED AT GLN 68 AND ILE 85. HELIX_ID: AB,BOTH TERMINI ARE IN 3_10 ...HELIX HELIX HELIX_ID: AA,DISTORTED AT GLN 68 AND ILE 85. HELIX_ID: AB,BOTH TERMINI ARE IN 3_10 HELIX CONFORMATION. HELIX_ID: AD,FROM ALA 138 ONWARDS HELIX IS IN 3/10 CONFORMATION. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 76.5 KB | Display | ![]() |
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PDB format | ![]() | 56.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 40252.863 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-GSP / |
#4: Water | ChemComp-HOH / |
Nonpolymer details | COMPND GTP-GAMMA-S IS NON-HYDROLYZAB |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 50.32 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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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
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 16167 / % possible obs: 97.1 % / Observed criterion σ(I): 0 |
Reflection | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 15 Å / % possible obs: 97.2 % / Redundancy: 3.3 % / Num. measured all: 58697 / Rmerge(I) obs: 0.041 |
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Processing
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Refinement | Resolution: 2.3→8 Å / σ(F): 1
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Displacement parameters | Biso mean: 12.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 8 Å / Rfactor obs: 0.23 / Rfactor Rfree: 0.31 / Rfactor Rwork: 0.23 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.588 |