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Open data
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Basic information
Entry | Database: PDB / ID: 4orb | ||||||
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Title | Crystal structure of mouse calcineurin | ||||||
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![]() | HYDROLASE/METAL BINDING PROTEIN / Calmodulin-binding / HYDROLASE-METAL BINDING PROTEIN complex | ||||||
Function / homology | ![]() negative regulation of chromatin binding / Activation of BAD and translocation to mitochondria / : / CLEC7A (Dectin-1) induces NFAT activation / calcium-dependent protein serine/threonine phosphatase activity / Calcineurin activates NFAT / cellular response to xenobiotic stimulus => GO:0071466 / positive regulation of cardiac muscle hypertrophy in response to stress / calmodulin-dependent protein phosphatase activity / calcineurin complex ...negative regulation of chromatin binding / Activation of BAD and translocation to mitochondria / : / CLEC7A (Dectin-1) induces NFAT activation / calcium-dependent protein serine/threonine phosphatase activity / Calcineurin activates NFAT / cellular response to xenobiotic stimulus => GO:0071466 / positive regulation of cardiac muscle hypertrophy in response to stress / calmodulin-dependent protein phosphatase activity / calcineurin complex / positive regulation of connective tissue replacement / negative regulation of dendrite morphogenesis / calcineurin-mediated signaling / Ca2+ pathway / slit diaphragm / FCERI mediated Ca+2 mobilization / : / peptidyl-serine dephosphorylation / lung epithelial cell differentiation / calcineurin-NFAT signaling cascade / transition between fast and slow fiber / myelination in peripheral nervous system / cardiac muscle hypertrophy in response to stress / negative regulation of miRNA processing / cyclosporin A binding / branching involved in blood vessel morphogenesis / postsynaptic modulation of chemical synaptic transmission / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase / positive regulation of cardiac muscle hypertrophy / positive regulation of endocytosis / phosphoprotein phosphatase activity / protein localization to nucleus / positive regulation of cell adhesion / epithelial to mesenchymal transition / phosphatase binding / negative regulation of insulin secretion / multicellular organismal response to stress / Schwann cell development / skeletal muscle fiber development / dephosphorylation / response to amphetamine / excitatory postsynaptic potential / protein dephosphorylation / calcium-mediated signaling / cellular response to glucose stimulus / Schaffer collateral - CA1 synapse / modulation of chemical synaptic transmission / brain development / cytoplasmic side of plasma membrane / sarcolemma / positive regulation of DNA-binding transcription factor activity / Z disc / response to calcium ion / G1/S transition of mitotic cell cycle / protein import into nucleus / calcium ion transport / heart development / ATPase binding / postsynapse / dendritic spine / protein dimerization activity / calmodulin binding / positive regulation of cell migration / protein domain specific binding / negative regulation of gene expression / glutamatergic synapse / synapse / calcium ion binding / protein-containing complex binding / positive regulation of gene expression / enzyme binding / positive regulation of transcription by RNA polymerase II / mitochondrion / nucleoplasm / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ma, L. / Li, S.J. / Wang, J. / Wu, J.W. / Wang, Z.X. | ||||||
![]() | ![]() Title: Cooperative autoinhibition and multi-level activation mechanisms of calcineurin Authors: Li, S.J. / Ma, L. / Wang, J. / Lu, C. / Wang, J. / Wu, J.W. / Wang, Z.X. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 237.3 KB | Display | ![]() |
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PDB format | ![]() | 188.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 443.3 KB | Display | ![]() |
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Full document | ![]() | 451.4 KB | Display | |
Data in XML | ![]() | 21.1 KB | Display | |
Data in CIF | ![]() | 28.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4or9C ![]() 4oraC ![]() 4orcC ![]() 1auiS C: citing same article ( S: Starting model for refinement |
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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
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 58754.734 Da / Num. of mol.: 1 / Fragment: catalytic subunit Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P63328, protein-serine/threonine phosphatase |
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#2: Protein | Mass: 19322.904 Da / Num. of mol.: 1 / Fragment: regulatory subunit Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Non-polymers , 4 types, 21 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/FE.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/FE.gif)
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![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-ZN / | ||
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#4: Chemical | ChemComp-FE / | ||
#5: Chemical | ChemComp-CA / #6: Water | ChemComp-HOH / | |
-Details
Sequence details | AMINO ACIDS (447-456) ARE MISSING BECAUSE THIS SEQUENCE CORRESPOND |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.96 Å3/Da / Density % sol: 58.39 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 6.1 Details: 100mM MES, pH 6.1, 18% PEG3350, 8% Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX225HE / Detector: CCD / Date: Jul 21, 2010 |
Radiation | Monochromator: rotated-inclined double-crystal monochromator Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→40 Å / Num. all: 17090 / Num. obs: 17038 / % possible obs: 98 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 4.3 % / Biso Wilson estimate: 61.1 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 3.1→3.21 Å / Redundancy: 4 % / Rmerge(I) obs: 0.606 / Mean I/σ(I) obs: 2.273 / Num. unique all: 1587 / % possible all: 92.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1AUI Resolution: 3.108→39.691 Å / SU ML: 0.42 / σ(F): 1.35 / Phase error: 22.86 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 37.512 Å2 / ksol: 0.377 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 3.108→39.691 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 6
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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