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- PDB-1vr2: HUMAN VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 (KDR) KINASE ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1vr2 | ||||||
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Title | HUMAN VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 (KDR) KINASE DOMAIN | ||||||
![]() | PROTEIN (VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR KINASE) | ||||||
![]() | TRANSFERASE / TYROSINE KINASE | ||||||
Function / homology | ![]() blood vessel endothelial cell differentiation / cellular response to hydrogen sulfide / regulation of bone development / Signaling by membrane-tethered fusions of PDGFRA or PDGFRB / vascular endothelial growth factor binding / Neurophilin interactions with VEGF and VEGFR / vascular endothelial growth factor receptor-2 signaling pathway / VEGF binds to VEGFR leading to receptor dimerization / endothelium development / endocardium development ...blood vessel endothelial cell differentiation / cellular response to hydrogen sulfide / regulation of bone development / Signaling by membrane-tethered fusions of PDGFRA or PDGFRB / vascular endothelial growth factor binding / Neurophilin interactions with VEGF and VEGFR / vascular endothelial growth factor receptor-2 signaling pathway / VEGF binds to VEGFR leading to receptor dimerization / endothelium development / endocardium development / vascular wound healing / regulation of hematopoietic progenitor cell differentiation / vascular endothelial growth factor receptor activity / post-embryonic camera-type eye morphogenesis / endothelial cell differentiation / positive regulation of vasculogenesis / mesenchymal cell proliferation / lymph vessel development / positive regulation of BMP signaling pathway / surfactant homeostasis / cell migration involved in sprouting angiogenesis / anchoring junction / epithelial cell maturation / positive regulation of positive chemotaxis / embryonic hemopoiesis / vascular endothelial growth factor signaling pathway / positive regulation of mesenchymal cell proliferation / positive regulation of endothelial cell chemotaxis / positive regulation of mitochondrial depolarization / branching involved in blood vessel morphogenesis / positive regulation of cell migration involved in sprouting angiogenesis / positive regulation of mitochondrial fission / 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 / cell fate commitment / vasculogenesis / calcium ion homeostasis / Integrin cell surface interactions / coreceptor activity / vascular endothelial growth factor receptor signaling pathway / negative regulation of endothelial cell apoptotic process / peptidyl-tyrosine autophosphorylation / ovarian follicle development / positive regulation of endothelial cell proliferation / cell surface receptor protein tyrosine kinase signaling pathway / 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 / positive regulation of angiogenesis / cell migration / integrin binding / cell junction / regulation of cell shape / protein tyrosine kinase activity / angiogenesis / negative regulation of neuron apoptotic process / positive regulation of MAPK cascade / protein autophosphorylation / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of ERK1 and ERK2 cascade / early endosome / receptor complex / 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 | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Mctigue, M. / Wickersham, J. / Pinko, C. / Showalter, R. / Parast, C. / Tempczyk-Russell, A. / Gehring, M. / Mroczkowski, B. / Kan, C. / Villafranca, J. / Appelt, K. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 70.6 KB | Display | ![]() |
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PDB format | ![]() | 50.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 371.4 KB | Display | ![]() |
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Full document | ![]() | 381 KB | Display | |
Data in XML | ![]() | 8 KB | Display | |
Data in CIF | ![]() | 12.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1fgkS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() |
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 |
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Processing
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Refinement | Method to determine structure: ![]() 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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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