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Yorodumi- PDB-5mk0: Crystal structure of the His Domain Protein Tyrosine Phosphatase ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5mk0 | ||||||||||||
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Title | Crystal structure of the His Domain Protein Tyrosine Phosphatase (HD-PTP/PTPN23) Bro1 domain (Endofin peptide complex) | ||||||||||||
Components |
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Keywords | HYDROLASE / ESCRT-III Endofin | ||||||||||||
Function / homology | Function and homology information positive regulation of homophilic cell adhesion / positive regulation of adherens junction organization / 1-phosphatidylinositol binding / positive regulation of Wnt protein secretion / positive regulation of early endosome to late endosome transport / negative regulation of epithelial cell migration / vesicle organization / protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / protein targeting to lysosome / Signaling by BMP ...positive regulation of homophilic cell adhesion / positive regulation of adherens junction organization / 1-phosphatidylinositol binding / positive regulation of Wnt protein secretion / positive regulation of early endosome to late endosome transport / negative regulation of epithelial cell migration / vesicle organization / protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / protein targeting to lysosome / Signaling by BMP / early endosome to late endosome transport / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / endocytic recycling / Interleukin-37 signaling / endosomal transport / phosphatidylinositol-3,4,5-trisphosphate binding / regulation of endocytosis / cilium assembly / protein-tyrosine-phosphatase / ciliary basal body / protein tyrosine phosphatase activity / early endosome membrane / early endosome / nuclear body / endosome / intracellular membrane-bounded organelle / protein kinase binding / signal transduction / extracellular exosome / nucleoplasm / nucleus / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.765 Å | ||||||||||||
Authors | Levy, C. / Gahloth, D. | ||||||||||||
Funding support | United Kingdom, 3items
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Citation | Journal: Structure / Year: 2017 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5mk0.cif.gz | 168.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5mk0.ent.gz | 133.2 KB | Display | PDB format |
PDBx/mmJSON format | 5mk0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5mk0_validation.pdf.gz | 437.2 KB | Display | wwPDB validaton report |
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Full document | 5mk0_full_validation.pdf.gz | 439 KB | Display | |
Data in XML | 5mk0_validation.xml.gz | 31 KB | Display | |
Data in CIF | 5mk0_validation.cif.gz | 46.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mk/5mk0 ftp://data.pdbj.org/pub/pdb/validation_reports/mk/5mk0 | HTTPS FTP |
-Related structure data
Related structure data | 5mjyC 5mjzC 5mk1C 5mk2C 5mk3C 3rauS 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 40719.941 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PTPN23, KIAA1471 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9H3S7, protein-tyrosine-phosphatase #2: Protein/peptide | Mass: 2566.792 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q7Z3T8 #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.54 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop Details: 0.2 M Ammonium tartrate dibasic, 20% PEG3350 and 0.1 M MMT buffer pH 9.0, 25% PEG1500 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9762 Å |
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: 1.765→41.19 Å / Num. obs: 69302 / % possible obs: 96.48 % / Redundancy: 2.2 % / CC1/2: 0.995 / Rmerge(I) obs: 0.0544 / Net I/σ(I): 10.2 |
Reflection shell | Resolution: 1.765→1.828 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.293 / Mean I/σ(I) obs: 3.23 / CC1/2: 0.975 / % possible all: 93.55 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3RAU Resolution: 1.765→41.19 Å / SU ML: 0.16 / Cross valid method: FREE R-VALUE / σ(F): 2.19 / Phase error: 20.42
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.765→41.19 Å
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Refine LS restraints |
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LS refinement shell |
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