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- PDB-1b6c: CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF-BET... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1b6c | ||||||
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Title | CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF-BETA RECEPTOR IN COMPLEX WITH FKBP12 | ||||||
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![]() | COMPLEX (ISOMERASE/PROTEIN KINASE) / COMPLEX (ISOMERASE-PROTEIN KINASE) / RECEPTOR SERINE/THREONINE KINASE / COMPLEX (ISOMERASE-PROTEIN KINASE) complex | ||||||
Function / homology | ![]() extracellular structure organization / epicardium morphogenesis / parathyroid gland development / transforming growth factor beta ligand-receptor complex / regulation of cardiac muscle cell proliferation / positive regulation of tight junction disassembly / myofibroblast differentiation / positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation / TGFBR2 Kinase Domain Mutants in Cancer / transforming growth factor beta receptor activity ...extracellular structure organization / epicardium morphogenesis / parathyroid gland development / transforming growth factor beta ligand-receptor complex / regulation of cardiac muscle cell proliferation / positive regulation of tight junction disassembly / myofibroblast differentiation / positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation / TGFBR2 Kinase Domain Mutants in Cancer / transforming growth factor beta receptor activity / positive regulation of mesenchymal stem cell proliferation / ventricular compact myocardium morphogenesis / SMAD2/3 Phosphorylation Motif Mutants in Cancer / TGFBR1 KD Mutants in Cancer / macrolide binding / positive regulation of vasculature development / regulation of epithelial to mesenchymal transition / activin receptor binding / activin receptor activity, type I / cytoplasmic side of membrane / cardiac epithelial to mesenchymal transition / mesenchymal cell differentiation / transforming growth factor beta receptor activity, type I / activin receptor complex / neuron fate commitment / positive regulation of extracellular matrix assembly / signaling receptor inhibitor activity / transforming growth factor beta receptor binding / type II transforming growth factor beta receptor binding / TGFBR1 LBD Mutants in Cancer / receptor protein serine/threonine kinase / germ cell migration / angiogenesis involved in coronary vascular morphogenesis / transmembrane receptor protein serine/threonine kinase activity / pharyngeal system development / activin binding / type I transforming growth factor beta receptor binding / coronary artery morphogenesis / activin receptor signaling pathway / negative regulation of activin receptor signaling pathway / ventricular trabecula myocardium morphogenesis / filopodium assembly / heart trabecula formation / transforming growth factor beta binding / response to cholesterol / embryonic cranial skeleton morphogenesis / terminal cisterna / ryanodine receptor complex / I-SMAD binding / collagen fibril organization / negative regulation of chondrocyte differentiation / regulation of amyloid precursor protein catabolic process / endothelial cell activation / skeletal system morphogenesis / endothelial cell proliferation / lens development in camera-type eye / protein maturation by protein folding / positive regulation of filopodium assembly / anterior/posterior pattern specification / ventricular cardiac muscle tissue morphogenesis / 'de novo' protein folding / artery morphogenesis / negative regulation of phosphoprotein phosphatase activity / ventricular septum morphogenesis / FK506 binding / roof of mouth development / SMAD binding / mTORC1-mediated signalling / TGF-beta receptor signaling activates SMADs / negative regulation of endothelial cell proliferation / positive regulation of SMAD protein signal transduction / blastocyst development / regulation of protein ubiquitination / Calcineurin activates NFAT / regulation of immune response / endothelial cell migration / bicellular tight junction / epithelial to mesenchymal transition / protein peptidyl-prolyl isomerization / positive regulation of epithelial to mesenchymal transition / heart morphogenesis / supramolecular fiber organization / regulation of ryanodine-sensitive calcium-release channel activity / positive regulation of stress fiber assembly / cellular response to transforming growth factor beta stimulus / positive regulation of endothelial cell proliferation / sarcoplasmic reticulum membrane / T cell activation / negative regulation of cell migration / Downregulation of TGF-beta receptor signaling / transforming growth factor beta receptor signaling pathway / post-embryonic development / thymus development / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / peptidylprolyl isomerase / kidney development / skeletal system development / sarcoplasmic reticulum / peptidyl-prolyl cis-trans isomerase activity / cell motility Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Huse, M. / Chen, Y.-G. / Massague, J. / Kuriyan, J. | ||||||
![]() | ![]() Title: Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12. Authors: Huse, M. / Chen, Y.G. / Massague, J. / Kuriyan, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 339.5 KB | Display | ![]() |
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PDB format | ![]() | 277.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 508.3 KB | Display | ![]() |
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Full document | ![]() | 561.5 KB | Display | |
Data in XML | ![]() | 65.9 KB | Display | |
Data in CIF | ![]() | 88.5 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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1 | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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5 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.999639, -0.026418, -0.004965), Vector: |
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Components
#1: Protein | Mass: 11836.508 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 38920.641 Da / Num. of mol.: 4 / Fragment: CYTOPLASMIC PORTION Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.5 / Details: pH 8.5 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 200 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Feb 1, 1998 / Details: MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→30 Å / Num. obs: 57740 / % possible obs: 98 % / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Rsym value: 0.08 / Net I/σ(I): 18 |
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 3.5 % / Mean I/σ(I) obs: 6 / Rsym value: 0.24 / % possible all: 97.7 |
Reflection | *PLUS Rmerge(I) obs: 0.08 |
Reflection shell | *PLUS % possible obs: 97.7 % / Rmerge(I) obs: 0.243 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.29 Å2
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Refinement step | Cycle: LAST / Resolution: 2.6→30 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.6→2.62 Å / Total num. of bins used: 50
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Xplor file |
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Software | *PLUS Name: CNS / Version: 0.3 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |