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Yorodumi- PDB-2pld: NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOL... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2pld | ||||||
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Title | NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOLIPASE C-GAMMA1 COMPLEXED WITH A HIGH AFFINITY BINDING PEPTIDE | ||||||
Components |
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Keywords | PHOSPHORIC DIESTER HYDROLASE | ||||||
Function / homology | Function and homology information platelet activating factor receptor activity / platelet-derived growth factor receptor activity / platelet-derived growth factor beta-receptor activity / cell migration involved in coronary angiogenesis / metanephric glomerular mesangial cell proliferation involved in metanephros development / positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway / smooth muscle cell chemotaxis / calcium-dependent phospholipase C activity / metanephric glomerular capillary formation / cell migration involved in vasculogenesis ...platelet activating factor receptor activity / platelet-derived growth factor receptor activity / platelet-derived growth factor beta-receptor activity / cell migration involved in coronary angiogenesis / metanephric glomerular mesangial cell proliferation involved in metanephros development / positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway / smooth muscle cell chemotaxis / calcium-dependent phospholipase C activity / metanephric glomerular capillary formation / cell migration involved in vasculogenesis / aorta morphogenesis / phosphoinositide phospholipase C / positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway / platelet-derived growth factor binding / phospholipid catabolic process / vascular endothelial growth factor binding / retina vasculature development in camera-type eye / cardiac myofibril assembly / phosphatidylinositol metabolic process / Signaling by PDGF / positive regulation of chemotaxis / phosphatidylinositol phospholipase C activity / COP9 signalosome / platelet-derived growth factor receptor binding / positive regulation of DNA biosynthetic process / positive regulation of epithelial cell migration / positive regulation of smooth muscle cell migration / positive regulation of calcium ion import / platelet-derived growth factor receptor-beta signaling pathway / phosphatidylinositol-mediated signaling / : / platelet-derived growth factor receptor signaling pathway / cellular response to epidermal growth factor stimulus / cellular response to vascular endothelial growth factor stimulus / : / release of sequestered calcium ion into cytosol / ruffle / positive regulation of calcium-mediated signaling / Downstream signal transduction / positive regulation of mitotic nuclear division / lysosomal lumen / positive regulation of smooth muscle cell proliferation / cell chemotaxis / positive regulation of MAP kinase activity / guanyl-nucleotide exchange factor activity / epidermal growth factor receptor signaling pathway / receptor protein-tyrosine kinase / regulation of actin cytoskeleton organization / ruffle membrane / peptidyl-tyrosine phosphorylation / Constitutive Signaling by Aberrant PI3K in Cancer / positive regulation of reactive oxygen species metabolic process / PIP3 activates AKT signaling / lamellipodium / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / protein tyrosine kinase activity / cytoplasmic vesicle / protein autophosphorylation / in utero embryonic development / receptor complex / positive regulation of ERK1 and ERK2 cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of cell migration / protein kinase activity / apical plasma membrane / intracellular membrane-bounded organelle / focal adhesion / signaling receptor binding / positive regulation of cell population proliferation / calcium ion binding / protein kinase binding / enzyme binding / Golgi apparatus / signal transduction / ATP binding / membrane / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Pascal, S.M. / Singer, A.U. / Gish, G. / Yamazaki, T. / Shoelson, S.E. / Pawson, T. / Kay, L.E. / Forman-Kay, J.D. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1994 Title: Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide. Authors: Pascal, S.M. / Singer, A.U. / Gish, G. / Yamazaki, T. / Shoelson, S.E. / Pawson, T. / Kay, L.E. / Forman-Kay, J.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2pld.cif.gz | 51.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2pld.ent.gz | 39.7 KB | Display | PDB format |
PDBx/mmJSON format | 2pld.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2pld_validation.pdf.gz | 353.4 KB | Display | wwPDB validaton report |
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Full document | 2pld_full_validation.pdf.gz | 359.1 KB | Display | |
Data in XML | 2pld_validation.xml.gz | 4.8 KB | Display | |
Data in CIF | 2pld_validation.cif.gz | 6.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pl/2pld ftp://data.pdbj.org/pub/pdb/validation_reports/pl/2pld | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Atom site foot note | 1: RESIDUES A 1 - A 10, A 99 - A 105, B 1 - B 2, AND B 11 - B 12 ARE DISORDERED IN SOLUTION; THEREFORE, COORDINATES DISPLAY LARGE RMSD VALUES FOR THESE ATOMS. | |||||||||
NMR ensembles |
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-Components
#1: Protein | Mass: 12275.924 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) References: UniProt: P08487, phosphoinositide phospholipase C |
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#2: Protein/peptide | Mass: 1480.532 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / References: UniProt: P09619 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
Software |
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NMR software | Name: X-PLOR / Developer: BRUNGER / Classification: refinement | ||||||||
NMR ensemble | Conformers submitted total number: 1 |