- PDB-1x5a: The solution structure of the second fibronectin type III domain ... -
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Basic information
Entry
Database: PDB / ID: 1x5a
Title
The solution structure of the second fibronectin type III domain of mouse Ephrin type-A receptor 1
Components
Ephrin type-A receptor 1
Keywords
STRUCTURAL GENOMICS / UNKNOWN FUNCTION / Tyrosine-protein kinase receptor / ESK / fibronectin type III (fn3) domain / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI
Function / homology
Function and homology information
EPH-Ephrin signaling / EPHA-mediated growth cone collapse / EPH-ephrin mediated repulsion of cells / ephrin receptor activity / transmembrane-ephrin receptor activity / positive regulation of kinase activity / activation of GTPase activity / positive regulation of cell-matrix adhesion / regulation of GTPase activity / plasma membrane => GO:0005886 ...EPH-Ephrin signaling / EPHA-mediated growth cone collapse / EPH-ephrin mediated repulsion of cells / ephrin receptor activity / transmembrane-ephrin receptor activity / positive regulation of kinase activity / activation of GTPase activity / positive regulation of cell-matrix adhesion / regulation of GTPase activity / plasma membrane => GO:0005886 / fibronectin binding / positive regulation of stress fiber assembly / cell surface receptor protein tyrosine kinase signaling pathway / transmembrane receptor protein tyrosine kinase activity / negative regulation of cell migration / substrate adhesion-dependent cell spreading / axon guidance / negative regulation of protein kinase activity / receptor protein-tyrosine kinase / peptidyl-tyrosine phosphorylation / positive regulation of angiogenesis / angiogenesis / protein autophosphorylation / cell surface receptor signaling pathway / receptor complex / protein kinase activity / positive regulation of cell migration / neuron projection / positive regulation of cell population proliferation / protein kinase binding / ATP binding / plasma membrane Similarity search - Function
Ephrin type-A receptor 1, ligand binding domain / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Tyrosine-protein kinase, receptor class V, conserved site / Ephrin receptor, transmembrane domain / Ephrin receptor ligand binding domain / Ephrin type-A receptor 2 transmembrane domain / Receptor tyrosine kinase class V signature 1. / Receptor tyrosine kinase class V signature 2. / Eph receptor ligand-binding domain profile. ...Ephrin type-A receptor 1, ligand binding domain / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Tyrosine-protein kinase, receptor class V, conserved site / Ephrin receptor, transmembrane domain / Ephrin receptor ligand binding domain / Ephrin type-A receptor 2 transmembrane domain / Receptor tyrosine kinase class V signature 1. / Receptor tyrosine kinase class V signature 2. / Eph receptor ligand-binding domain profile. / Ephrin receptor ligand binding domain / SAM domain (Sterile alpha motif) / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Growth factor receptor cysteine-rich domain superfamily / EGF-like domain signature 2. / Fibronectin type III domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Galactose-binding-like domain superfamily / Fibronectin type III / Fibronectin type III superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Immunoglobulins / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta Similarity search - Domain/homology
Conformer selection criteria: target function,structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20
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