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- PDB-1fqj: CRYSTAL STRUCTURE OF THE HETEROTRIMERIC COMPLEX OF THE RGS DOMAIN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1fqj | ||||||
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Title | CRYSTAL STRUCTURE OF THE HETEROTRIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, THE GAMMA SUBUNIT OF PHOSPHODIESTERASE AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(PDEGAMMA)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)] | ||||||
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Function / homology | ![]() sensory perception of umami taste / Extra-nuclear estrogen signaling / detection of light stimulus involved in visual perception / Adenylate cyclase inhibitory pathway / G protein-coupled receptor complex / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Slep, K.C. / Kercher, M.A. / He, W. / Cowan, C.W. / Wensel, T.G. / Sigler, P.B. | ||||||
![]() | ![]() Title: Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A. Authors: Slep, K.C. / Kercher, M.A. / He, W. / Cowan, C.W. / Wensel, T.G. / Sigler, P.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 207.7 KB | Display | ![]() |
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PDB format | ![]() | 172 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 976.3 KB | Display | ![]() |
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Full document | ![]() | 993.1 KB | Display | |
Data in XML | ![]() | 41.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
-Protein , 2 types, 4 molecules ADBE
#1: Protein | Mass: 37361.656 Da / Num. of mol.: 2 Fragment: UNP P04695 residues 26-215 and 295-350 linked via UNP P10824 residues 220-298 Source method: isolated from a genetically manipulated source Details: THE CHIMERA COMPRISES RESIDUES 26 TO 215 OF BOVINE GT, RESIDUES 220 TO 298 OF RAT GI1, AND RESIDUES 295 TO 350 OF BOVINE GT Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() Genus: Bos, Rattus ![]() ![]() ![]() ![]() #2: Protein | Mass: 17419.176 Da / Num. of mol.: 2 / Fragment: RGS DOMAIN UNP RESIDUES 276-422 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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-Protein/peptide , 1 types, 1 molecules C
#3: Protein/peptide | Mass: 4559.094 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 46-87 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() References: UniProt: P04972, ![]() |
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-Non-polymers , 4 types, 362 molecules 






#4: Chemical | #5: Chemical | #6: Chemical | ![]() #7: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 59 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 9 Details: 15.0% PEG8000, 200mM Tris pH9.0, 0.2% beta-ME, 1mM (NH4)2WS4, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 8 | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: APS-1 / Detector: CCD / Date: Sep 6, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.02→50 Å / Num. all: 2227054 / Num. obs: 93531 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Biso Wilson estimate: 8.5 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 19.5 |
Reflection shell | Resolution: 2.02→2.09 Å / Redundancy: 6.1 % / Rmerge(I) obs: 0.553 / Num. unique all: 2094 / % possible all: 99.7 |
Reflection | *PLUS Num. measured all: 2227054 / Rmerge(I) obs: 0.09 |
Reflection shell | *PLUS % possible obs: 99.7 % / Mean I/σ(I) obs: 4.4 |
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Processing
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Refinement | Resolution: 2.02→50 Å / Rfactor Rfree error: 0.002 / Data cutoff high absF: 2012134.44 / Data cutoff low absF: 0 / Isotropic thermal model: OVERALL / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 35.33 Å2 / ksol: 0.344 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.02→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.02→2.15 Å / Rfactor Rfree error: 0.007 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 50 Å / σ(F): 0 / % reflection Rfree: 9.8 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 33.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.342 / % reflection Rfree: 9.9 % / Rfactor Rwork: 0.306 / Rfactor obs: 0.319 |