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- PDB-1tl7: Complex Of Gs- With The Catalytic Domains Of Mammalian Adenylyl C... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tl7 | ||||||
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Title | Complex Of Gs- With The Catalytic Domains Of Mammalian Adenylyl Cyclase: Complex With 2'(3')-O-(N-methylanthraniloyl)-guanosine 5'-triphosphate and Mn | ||||||
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![]() | LYASE / adenylyl cyclase / Gsa / MANT-GTP | ||||||
Function / homology | ![]() Adenylate cyclase activating pathway / Hedgehog 'off' state / PKA activation / Adenylate cyclase inhibitory pathway / sensory perception of chemical stimulus / adenylate cyclase / regulation of insulin secretion involved in cellular response to glucose stimulus / cAMP biosynthetic process / G alpha (z) signalling events / adenylate cyclase activity ...Adenylate cyclase activating pathway / Hedgehog 'off' state / PKA activation / Adenylate cyclase inhibitory pathway / sensory perception of chemical stimulus / adenylate cyclase / regulation of insulin secretion involved in cellular response to glucose stimulus / cAMP biosynthetic process / G alpha (z) signalling events / adenylate cyclase activity / adenylate cyclase binding / mu-type opioid receptor binding / corticotropin-releasing hormone receptor 1 binding / D1 dopamine receptor binding / beta-2 adrenergic receptor binding / adenylate cyclase-activating adrenergic receptor signaling pathway / cellular response to forskolin / adenylate cyclase activator activity / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / cAMP-mediated signaling / ionotropic glutamate receptor binding / insulin-like growth factor receptor binding / G-protein beta/gamma-subunit complex binding / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / cilium / adenylate cyclase-activating dopamine receptor signaling pathway / heterotrimeric G-protein complex / manganese ion binding / positive regulation of cytosolic calcium ion concentration / intracellular signal transduction / membrane raft / GTPase activity / dendrite / GTP binding / magnesium ion binding / protein-containing complex / ATP binding / membrane / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mou, T.C. / Gille, A. / Seifert, R.J. / Sprang, S.R. | ||||||
![]() | ![]() Title: Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate. Authors: Mou, T.C. / Gille, A. / Fancy, D.A. / Seifert, R. / Sprang, S.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 164.4 KB | Display | ![]() |
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PDB format | ![]() | 123.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 30.4 KB | Display | |
Data in CIF | ![]() | 40.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1u0hC ![]() 1azsS S: Starting model for refinement C: citing same article ( |
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Similar 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
-Adenylate cyclase, type ... , 2 types, 2 molecules AB
#1: Protein | Mass: 24495.361 Da / Num. of mol.: 1 / Fragment: C1A Domain Of Adenylyl Cyclase Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 23717.033 Da / Num. of mol.: 1 / Fragment: C2A Domain Of Adenylyl Cyclase Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Protein , 1 types, 1 molecules C
#3: Protein | Mass: 46656.438 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 7 types, 25 molecules ![](data/chem/img/MN.gif)
![](data/chem/img/FOK.gif)
![](data/chem/img/ONM.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/GSP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/FOK.gif)
![](data/chem/img/ONM.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/GSP.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | #5: Chemical | ChemComp-FOK / | #6: Chemical | ChemComp-ONM / | #7: Chemical | ChemComp-MG / | #8: Chemical | ChemComp-CL / | #9: Chemical | ChemComp-GSP / | #10: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.1 Å3/Da / Density % sol: 60.1 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 7.5-7.8% PEG 8000, 0.5M NACL, 0.1M PHOSPHATE BUFFER, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: SBC-3 / Detector: CCD / Date: Nov 23, 2003 Details: Active area: 210 x 210 mm2 Pixel sizes: 0.079 mm (unbinned mode) and 0.159 mm (2 x 2 binned mode) Unbinned images: 3072 pixels x 3072 pixels 2 x 2 Binned images: 1536 pixels x 1536 pixels |
Radiation | Monochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0393 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→50 Å / Num. all: 25538 / Num. obs: 22694 / Observed criterion σ(F): -2 / Observed criterion σ(I): -2 / Redundancy: 3.4 % / Rsym value: 0.162 / Net I/σ(I): 7.34 |
Reflection shell | Resolution: 2.8→2.91 Å / Redundancy: 1.7 % / Rmerge(I) obs: 0.379 / Mean I/σ(I) obs: 1.44 / Rsym value: 0.378 / % possible all: 66.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PBD entry 1AZS Resolution: 2.8→14.99 Å / Rfactor Rfree error: 0.009 / Data cutoff high absF: 167322.76 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 10 Å2 / ksol: 0.267686 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 45.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→14.99 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.97 Å / Rfactor Rfree error: 0.035 / Total num. of bins used: 6
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Xplor file |
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