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- PDB-8dc0: Rat Betaglycan Zona Pellucida Domain (ZPC) in complex with mini m... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8dc0 | |||||||||
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Title | Rat Betaglycan Zona Pellucida Domain (ZPC) in complex with mini monomer TGFb2 (mmTGF-b2-7M2R) | |||||||||
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![]() | CYTOKINE / Complex / Betaglycan / TGFb2 | |||||||||
Function / homology | ![]() TGFBR3 PTM regulation / TGFBR3 regulates FGF2 signaling / negative regulation of apoptotic process involved in morphogenesis / TGFBR3 regulates activin signaling / response to luteinizing hormone / FGFR1b ligand binding and activation / FGFR1c ligand binding and activation / TGF-beta receptor signaling activates SMADs / transforming growth factor beta receptor complex assembly / epicardium-derived cardiac fibroblast cell development ...TGFBR3 PTM regulation / TGFBR3 regulates FGF2 signaling / negative regulation of apoptotic process involved in morphogenesis / TGFBR3 regulates activin signaling / response to luteinizing hormone / FGFR1b ligand binding and activation / FGFR1c ligand binding and activation / TGF-beta receptor signaling activates SMADs / transforming growth factor beta receptor complex assembly / epicardium-derived cardiac fibroblast cell development / Signaling by BMP / regulation of timing of catagen / regulation of apoptotic process involved in outflow tract morphogenesis / negative regulation of epithelial to mesenchymal transition involved in endocardial cushion formation / substantia propria of cornea development / inhibin-betaglycan-ActRII complex / ascending aorta morphogenesis / muscular septum morphogenesis / cardioblast differentiation / uterine wall breakdown / definitive erythrocyte differentiation / positive regulation of timing of catagen / positive regulation of cardioblast differentiation / response to follicle-stimulating hormone / TGFBR3 regulates TGF-beta signaling / cardiac right ventricle morphogenesis / regulation of transforming growth factor beta2 production / BMP binding / atrial septum morphogenesis / pharyngeal arch artery morphogenesis / vasculogenesis involved in coronary vascular morphogenesis / positive regulation of heart contraction / type III transforming growth factor beta receptor binding / apoptotic process involved in morphogenesis / positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation / Signaling by Activin / negative regulation of macrophage cytokine production / transforming growth factor beta receptor activity / glial cell migration / ventricular compact myocardium morphogenesis / regulation of transforming growth factor beta receptor signaling pathway / secondary palate development / negative regulation of epithelial cell migration / somatic stem cell division / positive regulation of integrin biosynthetic process / atrial septum primum morphogenesis / endocardial cushion fusion / membranous septum morphogenesis / heart valve morphogenesis / TGFBR3 regulates TGF-beta signaling / cardiac epithelial to mesenchymal transition / eye development / signaling / positive regulation of stress-activated MAPK cascade / collagen metabolic process / embryonic digestive tract development / transforming growth factor beta receptor binding / cranial skeletal system development / neural retina development / type II transforming growth factor beta receptor binding / pulmonary valve morphogenesis / activation of protein kinase activity / transforming growth factor beta receptor activity, type III / activin binding / heart trabecula morphogenesis / outflow tract septum morphogenesis / ventricular trabecula myocardium morphogenesis / glycosaminoglycan binding / cell-cell junction organization / positive regulation of BMP signaling pathway / negative regulation of Ras protein signal transduction / heart trabecula formation / definitive hemopoiesis / transforming growth factor beta binding / collagen fibril organization / negative regulation of extracellular matrix assembly / embryonic limb morphogenesis / positive regulation of cell adhesion mediated by integrin / embryo development ending in birth or egg hatching / atrioventricular valve morphogenesis / odontogenesis / endocardial cushion morphogenesis / cardiac muscle cell proliferation / Molecules associated with elastic fibres / dopamine biosynthetic process / negative regulation of epithelial to mesenchymal transition / positive regulation of cell migration involved in sprouting angiogenesis / hair follicle morphogenesis / ventricular cardiac muscle tissue morphogenesis / generation of neurons / ventricular septum morphogenesis / negative regulation of SMAD protein signal transduction / positive regulation of Notch signaling pathway / blood vessel development / positive regulation of transforming growth factor beta receptor signaling pathway / SMAD binding / uterus development / fibroblast growth factor binding / inner ear development / roof of mouth development Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Wieteska, L. / Taylor, A.B. / Hinck, A.P. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Rat Betaglycan Zona Pellucida Domain (ZPC) in complex with mini monomer TGFb2 (mmTGF-b2-7M2R) Authors: Wieteska, L. / Taylor, A.B. / Hinck, A.P. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 136.3 KB | Display | ![]() |
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PDB format | ![]() | 93.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3qw9S ![]() 5tx4S S: Starting model for refinement |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 19915.881 Da / Num. of mol.: 1 / Fragment: ZPC domain (UNP residues 590-757) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 12944.903 Da / Num. of mol.: 1 / Fragment: mmTGF-b2-7m2r (UNP residues 303-414) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / |
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.71 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: 13% PEG4000, 0.1 M trisodium citrate, 10% ethylene glycol |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Feb 16, 2022 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97918 Å / Relative weight: 1 |
Reflection | Resolution: 1.93→66.74 Å / Num. obs: 26131 / % possible obs: 99.84 % / Redundancy: 13 % / Biso Wilson estimate: 38.51 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.1789 / Rrim(I) all: 0.1863 / Net I/σ(I): 9.27 |
Reflection shell | Resolution: 1.93→1.999 Å / Num. unique obs: 2560 / CC1/2: 0.404 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entries 3QW9 & 5TX4 Resolution: 1.93→66.74 Å / SU ML: 0.2869 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 30.7547 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 54.87 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.93→66.74 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group | Refine-ID: X-RAY DIFFRACTION
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