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Yorodumi- PDB-1ptv: CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WI... -
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-Basic information
Entry | Database: PDB / ID: 1ptv | ||||||
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Title | CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH PHOSPHOTYROSINE | ||||||
Components | PROTEIN TYROSINE PHOSPHATASE 1B | ||||||
Keywords | COMPLEX (HYDROLASE/PEPTIDE) / HYDROLASE / ACETYLATION / PHOSPHORYLATION / COMPLEX (HYDROLASE-PEPTIDE) COMPLEX | ||||||
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 PERK-mediated unfolded protein response / negative regulation of vascular endothelial growth factor receptor signaling pathway / 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 PERK-mediated unfolded protein response / negative regulation of vascular endothelial growth factor receptor signaling pathway / 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 / Growth hormone receptor signaling / MECP2 regulates neuronal receptors and channels / 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 / SYNCHROTRON / Resolution: 2.3 Å | ||||||
Authors | Barford, D. / Jia, Z. | ||||||
Citation | Journal: Science / Year: 1995 Title: Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Authors: Jia, Z. / Barford, D. / Flint, A.J. / Tonks, N.K. #1: Journal: Science / Year: 1994 Title: Crystal Structure of Human Protein Tyrosine Phosphatase 1B Authors: Barford, D. / Flint, A.J. / Tonks, N.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ptv.cif.gz | 78.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ptv.ent.gz | 58 KB | Display | PDB format |
PDBx/mmJSON format | 1ptv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ptv_validation.pdf.gz | 434.4 KB | Display | wwPDB validaton report |
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Full document | 1ptv_full_validation.pdf.gz | 439.4 KB | Display | |
Data in XML | 1ptv_validation.xml.gz | 8.1 KB | Display | |
Data in CIF | 1ptv_validation.cif.gz | 13.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pt/1ptv ftp://data.pdbj.org/pub/pdb/validation_reports/pt/1ptv | HTTPS FTP |
-Related 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: 37349.570 Da / Num. of mol.: 1 / Mutation: C215S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P18031, protein-tyrosine-phosphatase |
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#2: Chemical | ChemComp-PTR / |
#3: Water | ChemComp-HOH / |
Compound details | THE CATALYTIC RESIDUE IS CYS 215. IN THIS ENTRY RESIDUE 215 IS SER. |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.11 Å3/Da / Density % sol: 60.48 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion / Details: Barford, D., (1994) J. Mol. Biol., 239, 726. | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12C / Wavelength: 1.07 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE AREA DETECTOR / Date: Feb 1, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.07 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. obs: 21436 / % possible obs: 99.7 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.035 |
Reflection | *PLUS Num. measured all: 146758 |
-Processing
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Refinement | Resolution: 2.3→6 Å / σ(F): 2
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Displacement parameters | Biso mean: 25.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→6 Å
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Refine LS restraints |
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