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Yorodumi- PDB-1vr2: HUMAN VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 (KDR) KINASE ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1vr2 | ||||||
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Title | HUMAN VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 (KDR) KINASE DOMAIN | ||||||
Components | PROTEIN (VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR KINASE) | ||||||
Keywords | TRANSFERASE / TYROSINE KINASE | ||||||
Function / homology | Function and homology information blood vessel endothelial cell differentiation / cellular response to hydrogen sulfide / regulation of bone development / regulation of hematopoietic progenitor cell differentiation / Signaling by membrane-tethered fusions of PDGFRA or PDGFRB / endothelium development / Neurophilin interactions with VEGF and VEGFR / vascular endothelial growth factor binding / positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway / vascular endothelial growth factor receptor-2 signaling pathway ...blood vessel endothelial cell differentiation / cellular response to hydrogen sulfide / regulation of bone development / regulation of hematopoietic progenitor cell differentiation / Signaling by membrane-tethered fusions of PDGFRA or PDGFRB / endothelium development / Neurophilin interactions with VEGF and VEGFR / vascular endothelial growth factor binding / positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway / vascular endothelial growth factor receptor-2 signaling pathway / VEGF binds to VEGFR leading to receptor dimerization / endocardium development / vascular wound healing / vascular endothelial growth factor receptor activity / post-embryonic camera-type eye morphogenesis / endothelial cell differentiation / mesenchymal cell proliferation / positive regulation of vasculogenesis / lymph vessel development / positive regulation of BMP signaling pathway / surfactant homeostasis / epithelial cell maturation / anchoring junction / cell migration involved in sprouting angiogenesis / positive regulation of positive chemotaxis / embryonic hemopoiesis / vascular endothelial growth factor signaling pathway / positive regulation of mesenchymal cell proliferation / positive regulation of mitochondrial depolarization / positive regulation of mitochondrial fission / branching involved in blood vessel morphogenesis / positive regulation of cell migration involved in sprouting angiogenesis / lung alveolus development / positive regulation of stem cell proliferation / positive regulation of nitric-oxide synthase biosynthetic process / growth factor binding / sorting endosome / positive regulation of focal adhesion assembly / regulation of MAPK cascade / semaphorin-plexin signaling pathway / positive regulation of macroautophagy / : / positive regulation of blood vessel endothelial cell migration / cellular response to vascular endothelial growth factor stimulus / calcium ion homeostasis / cell fate commitment / vasculogenesis / Integrin cell surface interactions / vascular endothelial growth factor receptor signaling pathway / coreceptor activity / negative regulation of endothelial cell apoptotic process / peptidyl-tyrosine autophosphorylation / ovarian follicle development / positive regulation of endothelial cell proliferation / transmembrane receptor protein tyrosine kinase activity / positive regulation of endothelial cell migration / VEGFR2 mediated cell proliferation / epithelial cell proliferation / stem cell proliferation / Hsp90 protein binding / receptor protein-tyrosine kinase / VEGFA-VEGFR2 Pathway / peptidyl-tyrosine phosphorylation / cell surface receptor protein tyrosine kinase signaling pathway / positive regulation of angiogenesis / cell migration / integrin binding / cell junction / regulation of cell shape / angiogenesis / protein tyrosine kinase activity / negative regulation of neuron apoptotic process / positive regulation of MAPK cascade / protein autophosphorylation / positive regulation of ERK1 and ERK2 cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / early endosome / endosome / positive regulation of cell migration / cadherin binding / positive regulation of protein phosphorylation / membrane raft / external side of plasma membrane / negative regulation of gene expression / positive regulation of cell population proliferation / negative regulation of apoptotic process / Golgi apparatus / endoplasmic reticulum / extracellular region / ATP binding / identical protein binding / nucleus / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Mctigue, M. / Wickersham, J. / Pinko, C. / Showalter, R. / Parast, C. / Tempczyk-Russell, A. / Gehring, M. / Mroczkowski, B. / Kan, C. / Villafranca, J. / Appelt, K. | ||||||
Citation | Journal: Structure Fold.Des. / Year: 1999 Title: Crystal structure of the kinase domain of human vascular endothelial growth factor receptor 2: a key enzyme in angiogenesis. Authors: McTigue, M.A. / Wickersham, J.A. / Pinko, C. / Showalter, R.E. / Parast, C.V. / Tempczyk-Russell, A. / Gehring, M.R. / Mroczkowski, B. / Kan, C.C. / Villafranca, J.E. / Appelt, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1vr2.cif.gz | 70.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1vr2.ent.gz | 50.9 KB | Display | PDB format |
PDBx/mmJSON format | 1vr2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vr/1vr2 ftp://data.pdbj.org/pub/pdb/validation_reports/vr/1vr2 | HTTPS FTP |
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-Related structure data
Related structure data | 1fgkS S: Starting model for refinement |
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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: 36274.738 Da / Num. of mol.: 1 / Fragment: KINASE DOMAIN / Mutation: E990V Source method: isolated from a genetically manipulated source Details: PROTEIN WAS AUTOPHOSPHORYLATED AT RESIDUE 1059 PRIOR TO CRYSTALLIZATION. THIS PROTEIN CONSTRUCT CONTAINS THE KINASE DOMAIN WITH 50 RESIDUES (RESIDUES 940- 989) OF THE KINASE INSERT DOMAIN ...Details: PROTEIN WAS AUTOPHOSPHORYLATED AT RESIDUE 1059 PRIOR TO CRYSTALLIZATION. THIS PROTEIN CONSTRUCT CONTAINS THE KINASE DOMAIN WITH 50 RESIDUES (RESIDUES 940- 989) OF THE KINASE INSERT DOMAIN DELETED. THE PROTEIN ALSO CONTAINS A GLUTAMIC ACID TO VALINE MUTATION AT RESIDUE 990. Source: (gene. exp.) Homo sapiens (human) / Tissue: AORTA / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P35968, EC: 2.7.1.112 |
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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: 2.41 Å3/Da / Density % sol: 49.01 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.2 / Details: pH 7.2 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging dropDetails: drop consists of equal volume of protein and mother-liquor | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→15 Å / Num. obs: 17234 / % possible obs: 93 % / Redundancy: 3.9 % / Rsym value: 0.052 / Net I/σ(I): 23.6 |
Reflection shell | Resolution: 2.2→2.28 Å / Mean I/σ(I) obs: 3.4 / Rsym value: 0.196 / % possible all: 81.5 |
Reflection | *PLUS Rmerge(I) obs: 0.052 |
Reflection shell | *PLUS % possible obs: 81.5 % / Rmerge(I) obs: 0.196 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1FGK Resolution: 2.4→8 Å / Data cutoff high absF: 10000 / Data cutoff low absF: 1.1 / σ(F): 2
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Displacement parameters | Biso mean: 31.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→8 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: PARHCSDX.PRO / Topol file: TOPHCSDX.PRO | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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