+Open data
-Basic information
Entry | Database: PDB / ID: 1ab8 | ||||||
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Title | RAT TYPE II ADENYLYL CYCLASE C2 DOMAIN/FORSKOLIN COMPLEX | ||||||
Components | ADENYLYL CYCLASE | ||||||
Keywords | LYASE / ADENYLYL CYCLASE / PLASMID / COMPLEX (TRANSFERASE-INHIBITOR) | ||||||
Function / homology | Function and homology information Adenylate cyclase activating pathway / Hedgehog 'off' state / PKA activation / Adenylate cyclase inhibitory pathway / adenylate cyclase / cAMP biosynthetic process / G alpha (z) signalling events / adenylate cyclase activity / adenylate cyclase binding / cellular response to forskolin ...Adenylate cyclase activating pathway / Hedgehog 'off' state / PKA activation / Adenylate cyclase inhibitory pathway / adenylate cyclase / cAMP biosynthetic process / G alpha (z) signalling events / adenylate cyclase activity / adenylate cyclase binding / cellular response to forskolin / 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 / manganese ion binding / membrane raft / dendrite / magnesium ion binding / protein-containing complex / ATP binding / membrane / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 2.2 Å | ||||||
Authors | Zhang, G. / Hurley, J.H. | ||||||
Citation | Journal: Nature / Year: 1997 Title: Structure of the adenylyl cyclase catalytic core. Authors: Zhang, G. / Liu, Y. / Ruoho, A.E. / Hurley, J.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ab8.cif.gz | 86.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ab8.ent.gz | 65.1 KB | Display | PDB format |
PDBx/mmJSON format | 1ab8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ab/1ab8 ftp://data.pdbj.org/pub/pdb/validation_reports/ab/1ab8 | 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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2 |
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Unit cell |
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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.198769, -0.978716, -0.051049), Vector: |
-Components
#1: Protein | Mass: 24447.781 Da / Num. of mol.: 2 / Fragment: C2 DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: PPROEX-1 / Plasmid: PPROEX-1 / Species (production host): Escherichia coli / Gene (production host): PPROEX-1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 / Variant (production host): DE3 / References: UniProt: P26769, adenylate cyclase #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 55 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.9 Details: 1.1 M AM SO4, 0.1 M PHOSPHATE, PH 5.9, 2 % DMSO, 1 MM FORSKOLIN, 10 MM DTT, 80 MM NACL, 50 MM TRIS HCL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21-24 ℃ / Method: unknown / PH range low: 5.9 / PH range high: 5.8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.908 |
Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Dec 1, 1996 |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.908 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→40 Å / Num. obs: 17326 / % possible obs: 91 % / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Rmerge(I) obs: 0.067 / Rsym value: 0.067 / Net I/σ(I): 15 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 1 % / Mean I/σ(I) obs: 3 / % possible all: 40 |
Reflection | *PLUS Num. measured all: 51618 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 2.2→6 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 1.0E-5 / Isotropic thermal model: RESTRAINED / Cross valid method: FREE R / σ(F): 2 / Details: ANISOTROPIC DIFFRACTION
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Displacement parameters | Biso mean: 41 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati d res low obs: 6 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→6 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINED | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.8 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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