+Open data
-Basic information
Entry | Database: PDB / ID: 1t48 | ||||||
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Title | Allosteric Inhibition of Protein Tyrosine Phosphatase 1B | ||||||
Components | Protein-tyrosine phosphatase, non-receptor type 1 | ||||||
Keywords | HYDROLASE / Allosteric Inhibition / Protein Tyrosine Phosphatase 1B | ||||||
Function / homology | Function and homology information regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / positive regulation of receptor catabolic process / insulin receptor recycling / negative regulation of vascular endothelial growth factor receptor signaling pathway / negative regulation of PERK-mediated unfolded protein response / regulation of intracellular protein transport / IRE1-mediated unfolded protein response / cytoplasmic side of endoplasmic reticulum membrane ...regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / positive regulation of receptor catabolic process / insulin receptor recycling / negative regulation of vascular endothelial growth factor receptor signaling pathway / negative regulation of PERK-mediated unfolded protein response / regulation of intracellular protein transport / IRE1-mediated unfolded protein response / cytoplasmic side of endoplasmic reticulum membrane / platelet-derived growth factor receptor-beta signaling pathway / sorting endosome / mitochondrial crista / positive regulation of IRE1-mediated unfolded protein response / regulation of type I interferon-mediated signaling pathway / regulation of endocytosis / non-membrane spanning protein tyrosine phosphatase activity / positive regulation of protein tyrosine kinase activity / peptidyl-tyrosine dephosphorylation / Regulation of IFNA/IFNB signaling / regulation of signal transduction / cellular response to unfolded protein / growth hormone receptor signaling pathway via JAK-STAT / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of signal transduction / Regulation of IFNG signaling / MECP2 regulates neuronal receptors and channels / Growth hormone receptor signaling / endoplasmic reticulum unfolded protein response / positive regulation of JUN kinase activity / Insulin receptor recycling / negative regulation of insulin receptor signaling pathway / ephrin receptor binding / Integrin signaling / protein dephosphorylation / protein-tyrosine-phosphatase / negative regulation of MAP kinase activity / protein phosphatase 2A binding / protein tyrosine phosphatase activity / endosome lumen / insulin receptor binding / Negative regulation of MET activity / negative regulation of ERK1 and ERK2 cascade / receptor tyrosine kinase binding / insulin receptor signaling pathway / actin cytoskeleton organization / early endosome / mitochondrial matrix / cadherin binding / protein kinase binding / enzyme binding / endoplasmic reticulum / protein-containing complex / RNA binding / zinc ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Wiesmann, C. / Barr, K.J. / Kung, J. / Zhu, J. / Shen, W. / Fahr, B.J. / Zhong, M. / Erlanson, D.A. / Taylor, L. / Randal, M. ...Wiesmann, C. / Barr, K.J. / Kung, J. / Zhu, J. / Shen, W. / Fahr, B.J. / Zhong, M. / Erlanson, D.A. / Taylor, L. / Randal, M. / McDowell, R.S. / Hansen, S.K. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2004 Title: Allosteric inhibition of protein tyrosine phosphatase 1B Authors: Wiesmann, C. / Barr, K.J. / Kung, J. / Zhu, J. / Erlanson, D.A. / Shen, W. / Fahr, B.J. / Zhong, M. / Taylor, L. / Randal, M. / McDowell, R.S. / Hansen, S.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1t48.cif.gz | 76.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1t48.ent.gz | 55.9 KB | Display | PDB format |
PDBx/mmJSON format | 1t48.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1t48_validation.pdf.gz | 769.6 KB | Display | wwPDB validaton report |
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Full document | 1t48_full_validation.pdf.gz | 779.2 KB | Display | |
Data in XML | 1t48_validation.xml.gz | 16.2 KB | Display | |
Data in CIF | 1t48_validation.cif.gz | 22.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t4/1t48 ftp://data.pdbj.org/pub/pdb/validation_reports/t4/1t48 | HTTPS FTP |
-Related structure data
Related structure data | 1t49C 1t4jC 1ptyS 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: 34720.566 Da / Num. of mol.: 1 / Fragment: Residues 1-298 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PTPN1, PTP1B / Production host: Escherichia coli (E. coli) / References: UniProt: P18031, protein-tyrosine-phosphatase |
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#2: Chemical | ChemComp-BB3 / |
#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: 3.6 Å3/Da / Density % sol: 65.6 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / Details: VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.54 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Apr 17, 2001 / Details: mirrors |
Radiation | Monochromator: Yale Mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→19.78 Å / Num. all: 24798 / Num. obs: 24798 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rsym value: 0.08 |
Reflection shell | Resolution: 2.2→2.28 Å / % possible all: 99.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1PTY Resolution: 2.2→20 Å / SU B: 3.18255 / SU ML: 0.08027 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.21068 / ESU R Free: 0.18983 / Stereochemistry target values: maximum likelyhood
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Displacement parameters | Biso mean: 58.032 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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