+Open data
-Basic information
Entry | Database: PDB / ID: 1veu | ||||||
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Title | Crystal structure of the p14/MP1 complex at 2.15 A resolution | ||||||
Components |
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Keywords | SIGNALING PROTEIN/PROTEIN BINDING / profilin / scaffold / adaptor / SIGNALING PROTEIN-PROTEIN BINDING COMPLEX | ||||||
Function / homology | Function and homology information Energy dependent regulation of mTOR by LKB1-AMPK / MTOR signalling / Regulation of PTEN gene transcription / Macroautophagy / Amino acids regulate mTORC1 / regulation of cell-substrate junction organization / TP53 Regulates Metabolic Genes / mTORC1-mediated signalling / FNIP-folliculin RagC/D GAP / Ragulator complex ...Energy dependent regulation of mTOR by LKB1-AMPK / MTOR signalling / Regulation of PTEN gene transcription / Macroautophagy / Amino acids regulate mTORC1 / regulation of cell-substrate junction organization / TP53 Regulates Metabolic Genes / mTORC1-mediated signalling / FNIP-folliculin RagC/D GAP / Ragulator complex / MAP2K and MAPK activation / protein localization to cell junction / TORC1 signaling / fibroblast migration / kinase activator activity / positive regulation of TOR signaling / positive regulation of TORC1 signaling / Neutrophil degranulation / guanyl-nucleotide exchange factor activity / regulation of cell growth / cellular response to amino acid stimulus / protein localization / late endosome / late endosome membrane / positive regulation of MAPK cascade / molecular adaptor activity / lysosomal membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.15 Å | ||||||
Authors | Kurzbauer, R. / Teis, D. / Maurer-Stroh, S. / Eisenhaber, F. / Hekman, M. / Bourenkov, G.P. / Bartunik, H.D. / Huber, L.A. / Clausen, T. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2004 Title: Crystal structure of the p14/MP1 scaffolding complex: How a twin couple attaches mitogen- activated protein kinase signaling to late endosomes Authors: Kurzbauer, R. / Teis, D. / De Araujo, M.E. / Maurer-Stroh, S. / Eisenhaber, F. / Bourenkov, G.P. / Bartunik, H.D. / Hekman, M. / Rapp, U.R. / Huber, L.A. / Clausen, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1veu.cif.gz | 60.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1veu.ent.gz | 43.7 KB | Display | PDB format |
PDBx/mmJSON format | 1veu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1veu_validation.pdf.gz | 443 KB | Display | wwPDB validaton report |
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Full document | 1veu_full_validation.pdf.gz | 449.2 KB | Display | |
Data in XML | 1veu_validation.xml.gz | 12.3 KB | Display | |
Data in CIF | 1veu_validation.cif.gz | 16.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ve/1veu ftp://data.pdbj.org/pub/pdb/validation_reports/ve/1veu | HTTPS FTP |
-Related structure data
Related structure data | 1vetSC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 13614.563 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) / References: UniProt: O88653 |
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#2: Protein | Mass: 13781.953 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) / References: UniProt: Q9JHS3 |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.6 Å3/Da / Density % sol: 33 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: PEG4000, Tris, Magnesium Chloride, Sodium/Potassium Phosphate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 16, 2004 |
Radiation | Monochromator: filter / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→20 Å / Num. all: 33808 / Num. obs: 11596 / % possible obs: 94.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 2.15→2.23 Å / % possible all: 92.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1vet Resolution: 2.15→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.15→20 Å
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Refine LS restraints |
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