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Yorodumi- PDB-1z3k: Structural Insight into the Binding Diversity between the Tyr-Pho... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1z3k | ||||||
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Title | Structural Insight into the Binding Diversity between the Tyr-Phosphorylated Human EphrinBs and Nck2 SH2 Domain | ||||||
Components | Cytoplasmic protein NCK2Cytoplasm | ||||||
Keywords | Structural Genomics / Unknown Function / Nck2 / SH2 domain / Eph receptor-ephrin mediated signaling | ||||||
Function / homology | Function and homology information Regulation of cortical dendrite branching / negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation / positive regulation of peptidyl-serine dephosphorylation / positive regulation of translation in response to endoplasmic reticulum stress / positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / immunological synapse formation / dendritic spine development / cytoskeletal anchor activity / vesicle membrane / signal complex assembly ...Regulation of cortical dendrite branching / negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation / positive regulation of peptidyl-serine dephosphorylation / positive regulation of translation in response to endoplasmic reticulum stress / positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / immunological synapse formation / dendritic spine development / cytoskeletal anchor activity / vesicle membrane / signal complex assembly / Activation of RAC1 / Nephrin family interactions / Ephrin signaling / lamellipodium assembly / RHOV GTPase cycle / positive regulation of actin filament polymerization / negative regulation of PERK-mediated unfolded protein response / RHOU GTPase cycle / ephrin receptor signaling pathway / signaling adaptor activity / positive regulation of T cell proliferation / phosphotyrosine residue binding / T cell activation / Downstream signal transduction / actin filament organization / epidermal growth factor receptor signaling pathway / receptor tyrosine kinase binding / VEGFA-VEGFR2 Pathway / cell migration / signaling receptor complex adaptor activity / scaffold protein binding / postsynaptic density / negative regulation of cell population proliferation / protein-containing complex binding / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / signal transduction / positive regulation of transcription by RNA polymerase II / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
Authors | Ran, X. / Song, J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2005 Title: Structural insight into the binding diversity between the Tyr-phosphorylated human ephrinBs and Nck2 SH2 domain. Authors: Ran, X. / Song, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1z3k.cif.gz | 313.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1z3k.ent.gz | 259.2 KB | Display | PDB format |
PDBx/mmJSON format | 1z3k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z3/1z3k ftp://data.pdbj.org/pub/pdb/validation_reports/z3/1z3k | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11424.827 Da / Num. of mol.: 1 / Fragment: SH2 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: O43639 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Details | Contents: 0.5mM Nck2 SH2 domain U-15N,13C; 20mM phosphate buffer NA; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 6.8 / 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
Refinement | Method: distance geometry, simulated annealing / Software ordinal: 1 |
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NMR ensemble | Conformer selection criteria: structures accepted by CNS program with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |