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Yorodumi- PDB-1v5s: Solution structure of kinase associated domain 1 of mouse MAP/mic... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1v5s | ||||||
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Title | Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3 | ||||||
Components | MAP/microtubule affinity-regulating kinase 3 | ||||||
Keywords | TRANSFERASE / KA1 domain / ELKL motif / MARK3 / phosphorylation / STRUCTURAL GENOMICS / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information Negative regulation of MAPK pathway / RAF activation / MAP2K and MAPK activation / peptidyl-serine autophosphorylation / negative regulation of protein localization to nucleus / tau-protein kinase activity / negative regulation of hippo signaling / positive regulation of protein binding / peptidyl-serine phosphorylation / non-specific serine/threonine protein kinase ...Negative regulation of MAPK pathway / RAF activation / MAP2K and MAPK activation / peptidyl-serine autophosphorylation / negative regulation of protein localization to nucleus / tau-protein kinase activity / negative regulation of hippo signaling / positive regulation of protein binding / peptidyl-serine phosphorylation / non-specific serine/threonine protein kinase / intracellular signal transduction / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / dendrite / ATP binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Tochio, N. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3 Authors: Tochio, N. / Koshiba, S. / Inoue, M. / 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 | 1v5s.cif.gz | 771 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1v5s.ent.gz | 647.1 KB | Display | PDB format |
PDBx/mmJSON format | 1v5s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v5/1v5s ftp://data.pdbj.org/pub/pdb/validation_reports/v5/1v5s | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14277.152 Da / Num. of mol.: 1 / Fragment: Kinase associated domain 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: RIKEN cDNA 1600015G02 / Plasmid: P020417-25 / References: UniProt: Q03141, EC: 2.7.1.27 |
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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: 2.0mM KA1 domain U-15N, 13C; 20mM phosphate buffer NA; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 6.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
-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 |