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Open data
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Basic information
Entry | Database: PDB / ID: 2cm3 | ||||||
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Title | Structure of Protein Tyrosine Phosphatase 1B (C2) | ||||||
![]() | TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1 | ||||||
![]() | HYDROLASE / POLYMORPHISM / PHOSPHORYLATION / PROTEIN PHOSPHATASE / ENDOPLASMIC RETICULUM / OXIDATION / ACETYLATION / PHOSPHATASE | ||||||
Function / homology | ![]() regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / positive regulation of receptor catabolic process / insulin receptor recycling / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / 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 / positive regulation of receptor catabolic process / insulin receptor recycling / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / 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 / negative regulation of insulin receptor signaling pathway / Insulin receptor recycling / 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 / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Ala, P.J. / Gonneville, L. / Hillman, M.C. / Becker-Pasha, M. / Wei, M. / Reid, B.G. / Klabe, R. / Yue, E.W. / Wayland, B. / Douty, B. ...Ala, P.J. / Gonneville, L. / Hillman, M.C. / Becker-Pasha, M. / Wei, M. / Reid, B.G. / Klabe, R. / Yue, E.W. / Wayland, B. / Douty, B. / Combs, A.P. / Polam, P. / Wasserman, Z. / Bower, M. / Burn, T.C. / Hollis, G.F. / Wynn, R. | ||||||
![]() | ![]() Title: Structural Basis for Inhibition of Protein-Tyrosine Phosphatase 1B by Isothiazolidinone Heterocyclic Phosphonate Mimetics. Authors: Ala, P.J. / Gonneville, L. / Hillman, M.C. / Becker-Pasha, M. / Wei, M. / Reid, B.G. / Klabe, R. / Yue, E.W. / Wayland, B. / Douty, B. / Polam, P. / Wasserman, Z. / Bower, M. / Combs, A.P. / ...Authors: Ala, P.J. / Gonneville, L. / Hillman, M.C. / Becker-Pasha, M. / Wei, M. / Reid, B.G. / Klabe, R. / Yue, E.W. / Wayland, B. / Douty, B. / Polam, P. / Wasserman, Z. / Bower, M. / Combs, A.P. / Burn, T.C. / Hollis, G.F. / Wynn, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 138.1 KB | Display | ![]() |
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PDB format | ![]() | 107.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2cm2C ![]() 2cm7C ![]() 2cm8C ![]() 2cmaC ![]() 2cmbC ![]() 2cmcC ![]() 1eeoS 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 35549.445 Da / Num. of mol.: 2 / Fragment: CATALYTIC DOMAIN, RESIDUES 2-298 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Compound details | MAY PLAY AN IMPORTANT ROLE IN CKII- AND P60C-SRC-INDUCED SIGNAL TRANSDUCTI | Sequence details | THE SEQUENCE USED IN THE CRYSTALLIZATION EXPERIMENTS WAS 1-6XHIS-298. WHICH MEANS THAT THERE ARE ...THE SEQUENCE USED IN THE CRYSTALLIZ | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.55 % |
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Crystal grow | pH: 7 Details: 12-16% PEG 3000, 100 MM HEPES PH 7.0-8.0, 200 MM MAGNESIUM ACETATE, 2 MM TCEP |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Details: BLUE CONFOCAL MAX-FLUX MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→27 Å / Num. obs: 38991 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 14.8 |
Reflection shell | Resolution: 2.1→2.18 Å / Redundancy: 3.75 % / Rmerge(I) obs: 0.14 / Mean I/σ(I) obs: 5.6 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1EEO Resolution: 2.1→7 Å / Cross valid method: THROUGHOUT / σ(F): 3
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Solvent computation | Bsol: 280 Å2 / ksol: 0.8 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.1→7 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: PROTEIN_REP.PARAM / Topol file: ION.TOP |