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- PDB-1cjk: COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENY... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cjk | ||||||
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Title | COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH ADENOSINE 5'-(ALPHA THIO)-TRIPHOSPHATE (RP), MG, AND MN | ||||||
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![]() | LYASE/LYASE/SIGNALING PROTEIN / COMPLEX (LYASE-HYDROLASE) / HYDROLASE / SIGNAL TRANSDUCING PROTEIN / CYCLASE / EFFECTOR ENZYME / LYASE-LYASE-SIGNALING PROTEIN COMPLEX | ||||||
Function / homology | ![]() Adenylate cyclase activating pathway / Hedgehog 'off' state / PKA activation / Adenylate cyclase inhibitory pathway / sensory perception of chemical stimulus / adenylate cyclase / mu-type opioid receptor binding / regulation of insulin secretion involved in cellular response to glucose stimulus / corticotropin-releasing hormone receptor 1 binding / cAMP biosynthetic process ...Adenylate cyclase activating pathway / Hedgehog 'off' state / PKA activation / Adenylate cyclase inhibitory pathway / sensory perception of chemical stimulus / adenylate cyclase / mu-type opioid receptor binding / regulation of insulin secretion involved in cellular response to glucose stimulus / corticotropin-releasing hormone receptor 1 binding / cAMP biosynthetic process / G alpha (z) signalling events / adenylate cyclase activity / beta-2 adrenergic receptor binding / adenylate cyclase binding / D1 dopamine receptor binding / adenylate cyclase-activating adrenergic receptor signaling pathway / cellular response to forskolin / insulin-like growth factor receptor binding / adenylate cyclase activator activity / ionotropic glutamate receptor binding / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / cAMP-mediated signaling / 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 | ![]() ![]() ![]() | ||||||
![]() | Tesmer, J.J.G. / Sprang, S.R. | ||||||
![]() | ![]() Title: Two-metal-Ion catalysis in adenylyl cyclase. Authors: Tesmer, J.J. / Sunahara, R.K. / Johnson, R.A. / Gosselin, G. / Gilman, A.G. / Sprang, S.R. #1: ![]() Title: Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS. Authors: Tesmer, J.J. / Sunahara, R.K. / Gilman, A.G. / 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 | ![]() | 165.4 KB | Display | ![]() |
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PDB format | ![]() | 124.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1cjtC ![]() 1cjuC ![]() 1cjvC ![]() 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 / Mutation: V476M 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 / Fragment: TRYPSINIZED FRAGMENT / Mutation: N-TERMINAL HEXAHISTIDINE TAG Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 8 types, 42 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/FOK.gif)
![](data/chem/img/TAT.gif)
![](data/chem/img/MES.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/GSP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MN.gif)
![](data/chem/img/FOK.gif)
![](data/chem/img/TAT.gif)
![](data/chem/img/MES.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/GSP.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | #5: Chemical | ChemComp-MN / | #6: Chemical | ChemComp-FOK / | #7: Chemical | ChemComp-TAT / | #8: Chemical | ChemComp-MES / | #9: Chemical | ChemComp-CL / | #10: Chemical | ChemComp-GSP / | #11: 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: 58 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 5.6 Details: CRYSTALLIZED IN HANGING DROPS CONTAINING PROTEIN MIXED 1:1 WITH WELL SOLUTION OF 7.2-7.5% PEG 8000, 500MM NACL AND 100 MM PHOSPHATE BUFFER (PH 5.4-5.6), VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / Details: Tesmer, J.J., (1997) Science, 278, 1907. / PH range low: 5.6 / PH range high: 5.4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: ADSC QUANTUM 4 / Detector: CCD / Date: Aug 15, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.923 Å / Relative weight: 1 |
Reflection | Resolution: 3→40 Å / Num. obs: 21547 / % possible obs: 89.3 % / Observed criterion σ(I): -3 / Redundancy: 2.6 % / Rsym value: 0.144 / Net I/σ(I): 6.5 |
Reflection shell | Resolution: 3→3.16 Å / Redundancy: 2.6 % / Mean I/σ(I) obs: 2.6 / Rsym value: 0.518 / % possible all: 82.9 |
Reflection | *PLUS Rmerge(I) obs: 0.142 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1AZS Resolution: 3→15 Å / Rfactor Rfree error: 0.006 / Data cutoff high rms absF: 1748946.6 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: A BULK SOLVENT CORRECTION WAS USED REFLECTIONS WITH L>20 WERE OMITTED FROM REFINEMENT
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 10 Å2 / ksol: 0.2748 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 43.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3→3.11 Å / Rfactor Rfree error: 0.029 / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: CNS / Version: 0.5 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS % reflection Rfree: 9.8 % / Rfactor obs: 0.22 / Rfactor Rwork: 0.22 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 43.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.344 / % reflection Rfree: 9 % / Rfactor Rwork: 0.323 |