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- PDB-5mk3: Crystal structure of the His Domain Protein Tyrosine Phosphatase ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5mk3 | ||||||||||||
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Title | Crystal structure of the His Domain Protein Tyrosine Phosphatase (HD-PTP/PTPN23) Bro 1 domain (CHMP4C peptide complex structure) | ||||||||||||
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![]() | HYDROLASE / ESCRT-III CHMP4C | ||||||||||||
Function / homology | ![]() positive regulation of homophilic cell adhesion / positive regulation of adherens junction organization / mitotic cytokinesis checkpoint signaling / negative regulation of cytokinesis / ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway / positive regulation of Wnt protein secretion / positive regulation of early endosome to late endosome transport / abscission / amphisome membrane / multivesicular body-lysosome fusion ...positive regulation of homophilic cell adhesion / positive regulation of adherens junction organization / mitotic cytokinesis checkpoint signaling / negative regulation of cytokinesis / ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway / positive regulation of Wnt protein secretion / positive regulation of early endosome to late endosome transport / abscission / amphisome membrane / multivesicular body-lysosome fusion / vesicle fusion with vacuole / late endosome to lysosome transport / ESCRT III complex / kinetochore microtubule / negative regulation of epithelial cell migration / protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / late endosome to vacuole transport via multivesicular body sorting pathway / regulation of centrosome duplication / nuclear membrane reassembly / Sealing of the nuclear envelope (NE) by ESCRT-III / midbody abscission / multivesicular body sorting pathway / vesicle budding from membrane / membrane fission / early endosome to late endosome transport / plasma membrane repair / multivesicular body membrane / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / multivesicular body assembly / regulation of mitotic spindle assembly / endocytic recycling / Translation of Replicase and Assembly of the Replication Transcription Complex / Interleukin-37 signaling / Flemming body / mitotic metaphase chromosome alignment / Macroautophagy / nucleus organization / viral budding via host ESCRT complex / autophagosome membrane / autophagosome maturation / cilium assembly / Pyroptosis / nuclear pore / dephosphorylation / Endosomal Sorting Complex Required For Transport (ESCRT) / multivesicular body / protein-tyrosine-phosphatase / viral budding from plasma membrane / ciliary basal body / HCMV Late Events / protein tyrosine phosphatase activity / macroautophagy / Late endosomal microautophagy / Budding and maturation of HIV virion / cytoplasmic side of plasma membrane / kinetochore / autophagy / protein transport / Translation of Replicase and Assembly of the Replication Transcription Complex / midbody / early endosome / nuclear body / endosome / lysosomal membrane / intracellular membrane-bounded organelle / protein kinase binding / protein homodimerization activity / extracellular exosome / nucleoplasm / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Levy, C. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural Basis for Specific Interaction of TGF beta Signaling Regulators SARA/Endofin with HD-PTP. Authors: Gahloth, D. / Levy, C. / Walker, L. / Wunderley, L. / Mould, A.P. / Taylor, S. / Woodman, P. / Tabernero, L. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 312.5 KB | Display | ![]() |
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PDB format | ![]() | 253.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 477.7 KB | Display | ![]() |
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Full document | ![]() | 487.5 KB | Display | |
Data in XML | ![]() | 58.2 KB | Display | |
Data in CIF | ![]() | 83.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5mjyC ![]() 5mjzC ![]() 5mk0C ![]() 5mk1C ![]() 5mk2C ![]() 3rauS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 40719.941 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 2091.192 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) ![]() #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 40.33 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop Details: 0.2 M Potassium thiocyanate, 0.1 M Bis-Tris propane pH 6.5, 20% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jan 31, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9762 Å / Relative weight: 1 |
Reflection | Resolution: 2→49.92 Å / Num. obs: 88613 / % possible obs: 95.87 % / Redundancy: 2.2 % / CC1/2: 0.996 / Rmerge(I) obs: 0.0567 / Net I/σ(I): 11.96 |
Reflection shell | Resolution: 2→2.071 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.228 / Mean I/σ(I) obs: 4.22 / CC1/2: 0.949 / % possible all: 94.24 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3RAU Resolution: 2→49.92 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 2.19 / Phase error: 27.05
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→49.92 Å
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Refine LS restraints |
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LS refinement shell |
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