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- PDB-7mrz: Structure of GDF11 bound to fused ActRIIB-ECD and Alk4-ECD with A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7mrz | ||||||
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Title | Structure of GDF11 bound to fused ActRIIB-ECD and Alk4-ECD with Anti-ActRIIB Fab fragment | ||||||
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![]() | SIGNALING PROTEIN/IMMUNE SYSTEM / Growth factor / type I receptor / Transforming growth factor beta / type II receptor / ternary complex / GDF11 / SIGNALING PROTEIN / SIGNALING PROTEIN-IMMUNE SYSTEM complex | ||||||
Function / homology | ![]() spinal cord anterior/posterior patterning / type B pancreatic cell maturation / negative regulation of amacrine cell differentiation / Regulation of signaling by NODAL / inhibin binding / activin receptor activity, type II / amacrine cell differentiation / lymphatic endothelial cell differentiation / positive regulation of activin receptor signaling pathway / nodal signaling pathway ...spinal cord anterior/posterior patterning / type B pancreatic cell maturation / negative regulation of amacrine cell differentiation / Regulation of signaling by NODAL / inhibin binding / activin receptor activity, type II / amacrine cell differentiation / lymphatic endothelial cell differentiation / positive regulation of activin receptor signaling pathway / nodal signaling pathway / activin receptor activity / venous blood vessel development / lymphangiogenesis / retina vasculature development in camera-type eye / positive regulation of trophoblast cell migration / activin receptor activity, type I / embryonic foregut morphogenesis / activin receptor complex / camera-type eye morphogenesis / artery development / receptor protein serine/threonine kinase / transmembrane receptor protein serine/threonine kinase activity / Signaling by BMP / activin binding / activin receptor signaling pathway / SMAD protein signal transduction / Signaling by Activin / metanephros development / kinase activator activity / Signaling by NODAL / gastrulation with mouth forming second / pancreas development / determination of left/right symmetry / skeletal system morphogenesis / negative regulation of cold-induced thermogenesis / insulin secretion / anterior/posterior pattern specification / ureteric bud development / cell surface receptor protein serine/threonine kinase signaling pathway / organ growth / roof of mouth development / SMAD binding / growth factor binding / odontogenesis of dentin-containing tooth / mesoderm development / positive regulation of SMAD protein signal transduction / hair follicle development / blood vessel remodeling / BMP signaling pathway / positive regulation of bone mineralization / positive regulation of osteoblast differentiation / response to glucose / extrinsic apoptotic signaling pathway / protein serine/threonine/tyrosine kinase activity / post-embryonic development / positive regulation of erythrocyte differentiation / kidney development / skeletal system development / cytokine activity / peptidyl-threonine phosphorylation / growth factor activity / lung development / negative regulation of cell growth / cellular response to growth factor stimulus / G1/S transition of mitotic cell cycle / nervous system development / heart development / in utero embryonic development / cell population proliferation / protein autophosphorylation / receptor complex / phosphorylation / negative regulation of cell population proliferation / protein phosphorylation / negative regulation of gene expression / intracellular membrane-bounded organelle / protein serine/threonine kinase activity / ubiquitin protein ligase binding / positive regulation of gene expression / regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / cell surface / signal transduction / protein-containing complex / extracellular space / nucleoplasm / ATP binding / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Goebel, E.J. / Kattamuri, C. / Gipson, G.R. / Thompson, T.B. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structures of activin ligand traps using natural sets of type I and type II TGF beta receptors. Authors: Goebel, E.J. / Kattamuri, C. / Gipson, G.R. / Krishnan, L. / Chavez, M. / Czepnik, M. / Maguire, M.C. / Grenha, R. / Hakansson, M. / Logan, D.T. / Grinberg, A.V. / Sako, D. / Castonguay, R. ...Authors: Goebel, E.J. / Kattamuri, C. / Gipson, G.R. / Krishnan, L. / Chavez, M. / Czepnik, M. / Maguire, M.C. / Grenha, R. / Hakansson, M. / Logan, D.T. / Grinberg, A.V. / Sako, D. / Castonguay, R. / Kumar, R. / Thompson, T.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 502.4 KB | Display | ![]() |
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PDB format | ![]() | 347.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 491.9 KB | Display | ![]() |
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Full document | ![]() | 496.2 KB | Display | |
Data in XML | ![]() | 26.5 KB | Display | |
Data in CIF | ![]() | 35.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7olyC ![]() 6macS S: Starting model for refinement C: citing same article ( |
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Similar 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
-Protein , 2 types, 2 molecules AC
#1: Protein | Mass: 12471.309 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 27952.279 Da / Num. of mol.: 1 Fragment: Extracellular domains of both proteins in the fused construct Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q13705, UniProt: P36896, receptor protein serine/threonine kinase |
-Antibody , 2 types, 2 molecules XY
#3: Antibody | Mass: 23427.180 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#4: Antibody | Mass: 24203.885 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Sugars / Non-polymers , 2 types, 2 molecules ![](data/chem/img/NAG.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/SO4.gif)
#5: Sugar | ChemComp-NAG / |
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#6: Chemical | ChemComp-SO4 / |
-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.95 Å3/Da / Density % sol: 68.82 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: 0.1M HEPES, 0.9M ammonium sulfate, 0.9 M KCl |
-Data collection
Diffraction | Mean temperature: 80 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 8, 2018 | ||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.033202 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||
Reflection | Resolution: 3→49.51 Å / Num. obs: 29791 / % possible obs: 99 % / Redundancy: 8 % / Biso Wilson estimate: 88.97 Å2 / CC1/2: 0.992 / Rmerge(I) obs: 0.181 / Rpim(I) all: 0.052 / Rrim(I) all: 0.189 / Net I/σ(I): 8.1 / Num. measured all: 237557 / Scaling rejects: 252 | ||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6MAC Resolution: 3→48.06 Å / SU ML: 0.5519 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 29.4425 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 99.16 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→48.06 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -3.13491701418 Å / Origin y: -13.2630231103 Å / Origin z: -39.73890755 Å
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Refinement TLS group | Selection details: all |