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- PDB-2f2p: Structure of calmodulin bound to a calcineurin peptide: a new way... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2f2p | ||||||
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Title | Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode | ||||||
![]() | Calmodulin fused with calmodulin-binding domain of calcineurin | ||||||
![]() | METAL BINDING PROTEIN / EF-hands / calcium / calmodulin / calcineurin | ||||||
Function / homology | ![]() CLEC7A (Dectin-1) induces NFAT activation / Calcineurin activates NFAT / FCERI mediated Ca+2 mobilization / regulation of cell proliferation involved in kidney morphogenesis / positive regulation of glomerulus development / negative regulation of signaling / positive regulation of saliva secretion / calmodulin-dependent protein phosphatase activity / calcineurin complex / calcineurin-NFAT signaling cascade ...CLEC7A (Dectin-1) induces NFAT activation / Calcineurin activates NFAT / FCERI mediated Ca+2 mobilization / regulation of cell proliferation involved in kidney morphogenesis / positive regulation of glomerulus development / negative regulation of signaling / positive regulation of saliva secretion / calmodulin-dependent protein phosphatase activity / calcineurin complex / calcineurin-NFAT signaling cascade / renal filtration / positive regulation of osteoclast differentiation / Ca2+ pathway / myosin phosphatase activity / protein-serine/threonine phosphatase / positive regulation of activated T cell proliferation / positive regulation of ryanodine-sensitive calcium-release channel activity / negative regulation of ryanodine-sensitive calcium-release channel activity / epidermis development / positive regulation of osteoblast differentiation / skeletal muscle fiber development / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / enzyme regulator activity / dephosphorylation / keratinocyte differentiation / protein dephosphorylation / modulation of chemical synaptic transmission / sarcolemma / Z disc / spindle pole / response to calcium ion / dendritic spine / calmodulin binding / protein domain specific binding / calcium ion binding / protein-containing complex / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ye, Q. / Wong, A. / Jia, Z. | ||||||
![]() | ![]() Title: Structure of calmodulin bound to a calcineurin Peptide: a new way of making an old binding mode. Authors: Ye, Q. / Li, X. / Wong, A. / Wei, Q. / Jia, Z. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 81.8 KB | Display | ![]() |
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PDB format | ![]() | 61.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.9 KB | Display | ![]() |
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Full document | ![]() | 449.5 KB | Display | |
Data in XML | ![]() | 15.3 KB | Display | |
Data in CIF | ![]() | 20.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2f2oC ![]() 1cdmS 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
#1: Protein | Mass: 19925.254 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-CA / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.22 Å3/Da / Density % sol: 61.75 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / Details: VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.6→119.523 Å / Num. obs: 15901 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rsym value: 0.096 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1CDM Resolution: 2.6→50 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.6→50 Å
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