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- PDB-1tgk: HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000 -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tgk | ||||||
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Title | HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000 | ||||||
![]() | TRANSFORMING GROWTH FACTOR BETA 3 | ||||||
![]() | GROWTH FACTOR / MITOGEN / GLYCOPROTEIN | ||||||
Function / homology | ![]() uterine wall breakdown / detection of hypoxia / frontal suture morphogenesis / embryonic neurocranium morphogenesis / type III transforming growth factor beta receptor binding / positive regulation of tight junction disassembly / negative regulation of macrophage cytokine production / secondary palate development / response to laminar fluid shear stress / type II transforming growth factor beta receptor binding ...uterine wall breakdown / detection of hypoxia / frontal suture morphogenesis / embryonic neurocranium morphogenesis / type III transforming growth factor beta receptor binding / positive regulation of tight junction disassembly / negative regulation of macrophage cytokine production / secondary palate development / response to laminar fluid shear stress / type II transforming growth factor beta receptor binding / type I transforming growth factor beta receptor binding / mammary gland development / cell-cell junction organization / transforming growth factor beta binding / digestive tract development / face morphogenesis / odontogenesis / Molecules associated with elastic fibres / positive regulation of filopodium assembly / lung alveolus development / TGF-beta receptor signaling activates SMADs / negative regulation of vascular associated smooth muscle cell proliferation / positive regulation of SMAD protein signal transduction / inner ear development / positive regulation of cell division / ECM proteoglycans / positive regulation of collagen biosynthetic process / positive regulation of epithelial to mesenchymal transition / salivary gland morphogenesis / positive regulation of stress fiber assembly / T-tubule / transforming growth factor beta receptor signaling pathway / platelet alpha granule lumen / cytokine activity / response to progesterone / female pregnancy / positive regulation of protein secretion / negative regulation of transforming growth factor beta receptor signaling pathway / growth factor activity / response to estrogen / Platelet degranulation / regulation of cell population proliferation / collagen-containing extracellular matrix / in utero embryonic development / negative regulation of neuron apoptotic process / positive regulation of MAPK cascade / response to hypoxia / positive regulation of apoptotic process / negative regulation of cell population proliferation / intracellular membrane-bounded organelle / neuronal cell body / positive regulation of cell population proliferation / protein-containing complex binding / positive regulation of DNA-templated transcription / cell surface / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Mittl, P.R.E. / Priestle, J.P. / Gruetter, M.G. | ||||||
![]() | ![]() Title: The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding. Authors: Mittl, P.R. / Priestle, J.P. / Cox, D.A. / McMaster, G. / Cerletti, N. / Grutter, M.G. #1: ![]() Title: Refined Crystal Structure of Human Transforming Growth Factor Beta 2 at 1.95 A Resolution Authors: Schlunegger, M.P. / Grutter, M.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 27.6 KB | Display | ![]() |
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PDB format | ![]() | 21.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 414.3 KB | Display | ![]() |
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Full document | ![]() | 419.9 KB | Display | |
Data in XML | ![]() | 7 KB | Display | |
Data in CIF | ![]() | 8.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 12734.504 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: STRAIN DEPOSITED AT DEUTSCHE SAMMLUNG VON MIKROORGANISMEN, MASCHENRODER WEG 1B, 3300 BRAUNSCHWEIG, GERMANY, ACCESSION NUMBER DSM 5658 Gene: HTGF-BETA3 / Plasmid: PPLMU / Gene (production host): HTGF-BETA3 / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.08 Å3/Da / Density % sol: 74.94 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Details: PEG 4000 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20-22 ℃ / pH: 8.4 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: Dec 23, 1992 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 4232 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 9.7 % / Rmerge(I) obs: 0.132 |
Reflection | *PLUS Highest resolution: 3.3 Å / Lowest resolution: 9999 Å |
Reflection shell | *PLUS Highest resolution: 3.3 Å / Lowest resolution: 3.36 Å / % possible obs: 100 % |
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Processing
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Refinement | Resolution: 3.3→10 Å / σ(F): 0 /
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Displacement parameters | Biso mean: 40.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.35 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.3→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |