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- PDB-6sf3: Bone morphogenetic protein 10 (BMP10) in complex with extracellul... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6sf3 | ||||||||||||
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Title | Bone morphogenetic protein 10 (BMP10) in complex with extracellular domain of activin receptor-like kinase 1 (ALK1) at 2.3 Angstrom | ||||||||||||
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![]() | CYTOKINE / BMP10 / ALK1 / complex / signalling / TGFbeta / BMP | ||||||||||||
Function / homology | ![]() atrial cardiac muscle tissue morphogenesis / regulation of cardiac muscle hypertrophy in response to stress / lymphatic endothelial cell differentiation / positive regulation of sarcomere organization / positive regulation of cell proliferation involved in heart morphogenesis / negative regulation of endothelial cell differentiation / regulation of endothelial cell proliferation / dorsal aorta morphogenesis / positive regulation of epithelial cell differentiation / blood vessel maturation ...atrial cardiac muscle tissue morphogenesis / regulation of cardiac muscle hypertrophy in response to stress / lymphatic endothelial cell differentiation / positive regulation of sarcomere organization / positive regulation of cell proliferation involved in heart morphogenesis / negative regulation of endothelial cell differentiation / regulation of endothelial cell proliferation / dorsal aorta morphogenesis / positive regulation of epithelial cell differentiation / blood vessel maturation / venous blood vessel development / ventricular cardiac muscle cell development / positive regulation of cartilage development / telethonin binding / transforming growth factor beta receptor activity / lymphangiogenesis / positive regulation of chondrocyte differentiation / negative regulation of cardiac muscle hypertrophy / BMP receptor complex / retina vasculature development in camera-type eye / BMP receptor activity / blood vessel endothelial cell proliferation involved in sprouting angiogenesis / positive regulation of endothelial cell differentiation / activin receptor activity, type I / transforming growth factor beta receptor activity, type I / negative regulation of focal adhesion assembly / endothelial tube morphogenesis / positive regulation of bicellular tight junction assembly / regulation of blood vessel endothelial cell migration / artery development / receptor protein serine/threonine kinase / transmembrane receptor protein serine/threonine kinase activity / activin binding / Signaling by BMP / cellular response to BMP stimulus / activin receptor signaling pathway / receptor serine/threonine kinase binding / heart trabecula formation / adult heart development / positive regulation of BMP signaling pathway / negative regulation of cell adhesion / transforming growth factor beta binding / dorsal/ventral pattern formation / blood circulation / wound healing, spreading of epidermal cells / Molecules associated with elastic fibres / negative regulation of endothelial cell migration / cardiac muscle cell proliferation / ventricular cardiac muscle tissue morphogenesis / endocardial cushion morphogenesis / sarcomere organization / positive regulation of Notch signaling pathway / positive regulation of cardiac muscle hypertrophy / regulation of DNA replication / SMAD binding / negative regulation of endothelial cell proliferation / positive regulation of SMAD protein signal transduction / negative regulation of blood vessel endothelial cell migration / regulation of cardiac muscle contraction / blood vessel remodeling / BMP signaling pathway / positive regulation of cardiac muscle cell proliferation / cellular response to transforming growth factor beta stimulus / positive regulation of endothelial cell proliferation / transforming growth factor beta receptor signaling pathway / negative regulation of cell migration / kidney development / cytokine activity / growth factor activity / hormone activity / negative regulation of cell growth / cellular response to growth factor stimulus / regulation of blood pressure / Z disc / positive regulation of angiogenesis / heart development / angiogenesis / in utero embryonic development / response to hypoxia / cell adhesion / negative regulation of cell population proliferation / negative regulation of gene expression / protein serine/threonine kinase activity / neuronal cell body / dendrite / regulation of DNA-templated transcription / positive regulation of gene expression / protein kinase binding / positive regulation of DNA-templated transcription / cell surface / signal transduction / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / ATP binding / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Guo, J. / Yu, M. / Li, W. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms. Authors: Salmon, R.M. / Guo, J. / Wood, J.H. / Tong, Z. / Beech, J.S. / Lawera, A. / Yu, M. / Grainger, D.J. / Reckless, J. / Morrell, N.W. / Li, W. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 105.2 KB | Display | ![]() |
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PDB format | ![]() | 67.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6sf1SC ![]() 6sf2C 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
#1: Protein | Mass: 10788.126 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P37023, receptor protein serine/threonine kinase |
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#2: Protein | Mass: 12177.185 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.75 Å3/Da / Density % sol: 67.16 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 0.07 M Amino acids (0.014 M DL-Glutamic acids monohydrate; 0.014 M DL-Alanine; 0.014 M Glycine; 0.014 M DL-Lysine monohydrochloride; 0.014 M DL-Serine), 0.07 M Buffer System 3 (0.07 M ...Details: 0.07 M Amino acids (0.014 M DL-Glutamic acids monohydrate; 0.014 M DL-Alanine; 0.014 M Glycine; 0.014 M DL-Lysine monohydrochloride; 0.014 M DL-Serine), 0.07 M Buffer System 3 (0.07 M Tris(base)/BICINE), 35% Precipitant Mix 4 (9% v/v MPD, 9% w/v PEG 1000, 9% w/ PEG3350) |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 19, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.976 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→311.44 Å / Num. obs: 15103 / % possible obs: 99.9 % / Redundancy: 14.7 % / Biso Wilson estimate: 46.5309023868 Å2 / CC1/2: 0.994 / Rpim(I) all: 0.075 / Net I/σ(I): 7.4 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 15.1 % / Mean I/σ(I) obs: 1.6 / Num. unique obs: 1408 / CC1/2: 0.635 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6SF1 Resolution: 2.3000067422→51.9058333333 Å / SU ML: 0.358600350348 / Cross valid method: THROUGHOUT / σ(F): 1.33792944578 / Phase error: 27.5151156747
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 58.9737321218 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3000067422→51.9058333333 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: 21.4160126815 Å / Origin y: -17.6787951068 Å / Origin z: -35.6142750508 Å
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Refinement TLS group | Selection details: all |