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Yorodumi- PDB-2ed0: Solution structure of the SH3 domain of Abl interactor 2 (Abelson... -
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-Basic information
Entry | Database: PDB / ID: 2ed0 | ||||||
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Title | Solution structure of the SH3 domain of Abl interactor 2 (Abelson interactor 2) | ||||||
Components | Abl interactor 2 | ||||||
Keywords | SIGNALING PROTEIN / Coiled coil / Cytoskeleton / Nuclear protein / Phosphorylation / SH3 domain / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information SCAR complex / zonula adherens assembly / actin-based cell projection / positive regulation of Arp2/3 complex-mediated actin nucleation / lens fiber cell morphogenesis / filopodium tip / cytoskeletal anchor activity / regulation of dendritic spine morphogenesis / actin polymerization or depolymerization / proline-rich region binding ...SCAR complex / zonula adherens assembly / actin-based cell projection / positive regulation of Arp2/3 complex-mediated actin nucleation / lens fiber cell morphogenesis / filopodium tip / cytoskeletal anchor activity / regulation of dendritic spine morphogenesis / actin polymerization or depolymerization / proline-rich region binding / Rac protein signal transduction / RHO GTPases Activate WASPs and WAVEs / RAC2 GTPase cycle / RAC3 GTPase cycle / signaling adaptor activity / positive regulation of lamellipodium assembly / cytoskeleton organization / RAC1 GTPase cycle / adherens junction / FCGR3A-mediated phagocytosis / neuron migration / Regulation of actin dynamics for phagocytic cup formation / kinase binding / VEGFA-VEGFR2 Pathway / SH3 domain binding / peptidyl-tyrosine phosphorylation / cell migration / lamellipodium / dendritic spine / cytoskeleton / ubiquitin protein ligase binding / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Abe, H. / Tochio, N. / Miyamoto, K. / Saito, K. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the SH3 domain of Abl interactor 2 (Abelson interactor 2) Authors: Abe, H. / Tochio, N. / Miyamoto, K. / Saito, K. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ed0.cif.gz | 444.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ed0.ent.gz | 373.3 KB | Display | PDB format |
PDBx/mmJSON format | 2ed0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ed0_validation.pdf.gz | 340.5 KB | Display | wwPDB validaton report |
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Full document | 2ed0_full_validation.pdf.gz | 480.5 KB | Display | |
Data in XML | 2ed0_validation.xml.gz | 26.4 KB | Display | |
Data in CIF | 2ed0_validation.cif.gz | 40.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ed/2ed0 ftp://data.pdbj.org/pub/pdb/validation_reports/ed/2ed0 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8433.171 Da / Num. of mol.: 1 / Fragment: SH3 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: cell-free protein synthesis / Gene: ABI2 / Plasmid: P050704-12 / References: UniProt: Q9NYB9 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.73mM Protein; 20mM d-Tris-HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O, 90% H2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |