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Yorodumi- PDB-2hlq: Crystal Structure of the Extracellular Domain of the Type II BMP ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2hlq | ||||||
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Title | Crystal Structure of the Extracellular Domain of the Type II BMP Receptor | ||||||
Components | Bone morphogenetic protein receptor type-2 | ||||||
Keywords | TRANSFERASE / receptor / serine kinase / three-finger toxin / ligand binding domain | ||||||
Function / homology | Function and homology information : / semi-lunar valve development / : / activin receptor activity, type II / negative regulation of chondrocyte proliferation / lymphatic endothelial cell differentiation / regulation of lung blood pressure / pulmonary valve development / tricuspid valve morphogenesis / chondrocyte development ...: / semi-lunar valve development / : / activin receptor activity, type II / negative regulation of chondrocyte proliferation / lymphatic endothelial cell differentiation / regulation of lung blood pressure / pulmonary valve development / tricuspid valve morphogenesis / chondrocyte development / lung vasculature development / lymphangiogenesis / negative regulation of cell proliferation involved in heart valve morphogenesis / venous blood vessel development / pharyngeal arch artery morphogenesis / aortic valve development / BMP binding / proteoglycan biosynthetic process / maternal placenta development / negative regulation of muscle cell differentiation / atrial septum morphogenesis / endocardial cushion development / positive regulation of cartilage development / endochondral bone morphogenesis / transforming growth factor beta receptor activity / retina vasculature development in camera-type eye / mitral valve morphogenesis / BMP receptor activity / positive regulation of axon extension involved in axon guidance / artery development / receptor protein serine/threonine kinase / Signaling by BMP / cellular response to BMP stimulus / outflow tract septum morphogenesis / positive regulation of BMP signaling pathway / endothelial cell apoptotic process / negative regulation of DNA biosynthetic process / positive regulation of ossification / negative regulation of systemic arterial blood pressure / vasculature development / endothelial cell proliferation / limb development / anterior/posterior pattern specification / cell surface receptor protein serine/threonine kinase signaling pathway / negative regulation of vasoconstriction / lung alveolus development / ventricular septum morphogenesis / positive regulation of epithelial cell migration / blood vessel development / outflow tract morphogenesis / growth factor binding / plasma membrane => GO:0005886 / positive regulation of SMAD protein signal transduction / mesoderm formation / blood vessel remodeling / positive regulation of osteoblast differentiation / BMP signaling pathway / positive regulation of bone mineralization / clathrin-coated pit / protein tyrosine kinase binding / cellular response to starvation / positive regulation of endothelial cell proliferation / basal plasma membrane / positive regulation of endothelial cell migration / caveola / negative regulation of smooth muscle cell proliferation / adherens junction / brain development / negative regulation of cell growth / cellular response to growth factor stimulus / osteoblast differentiation / regulation of cell population proliferation / postsynaptic density / receptor complex / cadherin binding / apical plasma membrane / axon / phosphorylation / protein phosphorylation / protein serine/threonine kinase activity / dendrite / neuronal cell body / positive regulation of gene expression / cell surface / positive regulation of transcription by RNA polymerase II / extracellular space / nucleoplasm / ATP binding / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Ovis aries (sheep) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.45 Å | ||||||
Authors | Mace, P.D. / Cutfield, J.F. / Cutfield, S.M. | ||||||
Citation | Journal: Biochem.Biophys.Res.Commun. / Year: 2006 Title: High resolution structures of the bone morphogenetic protein type II receptor in two crystal forms: Implications for ligand binding Authors: Mace, P.D. / Cutfield, J.F. / Cutfield, S.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2hlq.cif.gz | 57.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2hlq.ent.gz | 40.4 KB | Display | PDB format |
PDBx/mmJSON format | 2hlq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hl/2hlq ftp://data.pdbj.org/pub/pdb/validation_reports/hl/2hlq | HTTPS FTP |
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-Related structure data
Related structure data | 2hlrSC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 11146.431 Da / Num. of mol.: 1 / Fragment: residues 32-131 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Ovis aries (sheep) / Gene: BMPRII / Plasmid: PET21A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: Q4ZG08, UniProt: Q13873*PLUS, receptor protein serine/threonine kinase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.73 Å3/Da / Density % sol: 29 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 0.1M Na Citrate, 15% PEG1500, 0.2M Mg acetate, pH 6.0, vapor diffusion, hanging drop, temperature 290K |
-Data collection
Diffraction | Mean temperature: 113 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-1 / Wavelength: 0.97946 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 10, 2006 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97946 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Redundancy: 3.8 % / Av σ(I) over netI: 9.7 / Number: 52347 / Rmerge(I) obs: 0.053 / Rsym value: 0.053 / D res high: 1.45 Å / D res low: 27.932 Å / Num. obs: 13746 / % possible obs: 96.7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Diffraction reflection shell |
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Reflection | Resolution: 1.45→27.932 Å / Num. obs: 13746 / % possible obs: 96.7 % / Redundancy: 3.8 % / Rmerge(I) obs: 0.053 / Rsym value: 0.053 / Net I/σ(I): 9.7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Phasing
Phasing MR |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2HLR Resolution: 1.45→22.54 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.936 / SU B: 2.734 / SU ML: 0.05 / Cross valid method: THROUGHOUT / ESU R: 0.123 / ESU R Free: 0.091 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 11.826 Å2
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Refinement step | Cycle: LAST / Resolution: 1.45→22.54 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.45→1.488 Å / Total num. of bins used: 20
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