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Open data
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Basic information
Entry | Database: PDB / ID: 1aui | ||||||
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Title | HUMAN CALCINEURIN HETERODIMER | ||||||
![]() | (SERINE/THREONINE PHOSPHATASE ...) x 2 | ||||||
![]() | HYDROLASE / PHOSPHATASE / IMMUNOSUPPRESSION | ||||||
Function / homology | ![]() negative regulation of angiotensin-activated signaling pathway / regulation of cell proliferation involved in kidney morphogenesis / calcium-dependent protein serine/threonine phosphatase regulator activity / positive regulation of glomerulus development / negative regulation of calcium ion import across plasma membrane / calcium-dependent protein serine/threonine phosphatase activity / protein serine/threonine phosphatase complex / negative regulation of signaling / positive regulation of saliva secretion / positive regulation of cardiac muscle hypertrophy in response to stress ...negative regulation of angiotensin-activated signaling pathway / regulation of cell proliferation involved in kidney morphogenesis / calcium-dependent protein serine/threonine phosphatase regulator activity / positive regulation of glomerulus development / negative regulation of calcium ion import across plasma membrane / calcium-dependent protein serine/threonine phosphatase activity / protein serine/threonine phosphatase complex / negative regulation of signaling / positive regulation of saliva secretion / positive regulation of cardiac muscle hypertrophy in response to stress / positive regulation of calcium ion import across plasma membrane / calmodulin-dependent protein phosphatase activity / calcineurin complex / positive regulation of connective tissue replacement / negative regulation of dendrite morphogenesis / calcineurin-mediated signaling / slit diaphragm / peptidyl-serine dephosphorylation / lung epithelial cell differentiation / calcineurin-NFAT signaling cascade / renal filtration / skeletal muscle tissue regeneration / regulation of synaptic vesicle cycle / transition between fast and slow fiber / positive regulation of calcineurin-NFAT signaling cascade / myelination in peripheral nervous system / positive regulation of osteoclast differentiation / cardiac muscle hypertrophy in response to stress / regulation of postsynaptic neurotransmitter receptor internalization / parallel fiber to Purkinje cell synapse / dendrite morphogenesis / cyclosporin A binding / myosin phosphatase activity / CLEC7A (Dectin-1) induces NFAT activation / branching involved in blood vessel morphogenesis / postsynaptic modulation of chemical synaptic transmission / extrinsic component of plasma membrane / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase / positive regulation of activated T cell proliferation / positive regulation of endocytosis / Calcineurin activates NFAT / positive regulation of cell adhesion / DARPP-32 events / Activation of BAD and translocation to mitochondria / epidermis development / epithelial to mesenchymal transition / phosphatase binding / negative regulation of insulin secretion / multicellular organismal response to stress / positive regulation of osteoblast differentiation / skeletal muscle fiber development / dephosphorylation / keratinocyte differentiation / response to amphetamine / T cell activation / excitatory postsynaptic potential / hippocampal mossy fiber to CA3 synapse / FCERI mediated Ca+2 mobilization / protein dephosphorylation / cellular response to glucose stimulus / wound healing / Schaffer collateral - CA1 synapse / modulation of chemical synaptic transmission / sarcolemma / Z disc / response to calcium ion / G1/S transition of mitotic cell cycle / protein import into nucleus / calcium ion transport / Ca2+ pathway / 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 / calcium ion binding / protein-containing complex binding / positive regulation of gene expression / enzyme binding / positive regulation of transcription by RNA polymerase II / mitochondrion / nucleoplasm / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Kissinger, C.R. / Parge, H.E. / Knighton, D.R. / Pelletier, L.A. / Lewis, C.T. / Tempczyk, A. / Villafranca, J.E. | ||||||
![]() | ![]() Title: Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Authors: Kissinger, C.R. / Parge, H.E. / Knighton, D.R. / Lewis, C.T. / Pelletier, L.A. / Tempczyk, A. / Kalish, V.J. / Tucker, K.D. / Showalter, R.E. / Moomaw, E.W. / Gastinel, L.N. / Habuka, N. / ...Authors: Kissinger, C.R. / Parge, H.E. / Knighton, D.R. / Lewis, C.T. / Pelletier, L.A. / Tempczyk, A. / Kalish, V.J. / Tucker, K.D. / Showalter, R.E. / Moomaw, E.W. / Gastinel, L.N. / Habuka, N. / Chen, X. / Maldonado, F. / Barker, J.E. / Bacquet, R. / Villafranca, J.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 137.9 KB | Display | ![]() |
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PDB format | ![]() | 104.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 377.6 KB | Display | ![]() |
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Full document | ![]() | 384.5 KB | Display | |
Data in XML | ![]() | 12.4 KB | Display | |
Data in CIF | ![]() | 21.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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
-SERINE/THREONINE PHOSPHATASE ... , 2 types, 2 molecules AB
#1: Protein | Mass: 58756.676 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q08209, protein-serine/threonine phosphatase |
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#2: Protein | Mass: 19191.709 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P63098, protein-serine/threonine phosphatase |
-Non-polymers , 4 types, 442 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)
![](data/chem/img/CA.gif)
![](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 / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56 % | |||||||||||||||
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Crystal grow | pH: 7.5 Details: PROTEIN WAS CRYSTALLIZED FROM 8% PEG 6000, 0.1M CACL2, 0.1M TES PH 7.5, 1 MM DTT. | |||||||||||||||
Crystal grow | *PLUS Method: unknown | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 87 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Oct 1, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→30 Å / Num. obs: 50007 / % possible obs: 92.5 % / Observed criterion σ(I): 0 / Redundancy: 4 % / Rsym value: 0.069 |
Reflection | *PLUS Rmerge(I) obs: 0.069 |
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Processing
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Refinement | Method to determine structure: MIR PLUS ANOMALOUS SCATTERING Resolution: 2.1→10 Å / Isotropic thermal model: UNRESTRAINED Details: SIDE CHAIN ATOMS WITHOUT DISCERNIBLE ELECTRON DENSITY HAVE BEEN MODELLED IN STEREOCHEMICALLY REASONABLE POSITIONS AND ASSIGNED OCCUPANCIES OF ZERO.
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Displacement parameters | Biso mean: 39.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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