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- PDB-1gwz: CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE PROTEIN TYROSINE... -

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Basic information

Entry
Database: PDB / ID: 1gwz
TitleCRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE PROTEIN TYROSINE PHOSPHATASE SHP-1
ComponentsSHP-1
KeywordsHYDROLASE / PROTEIN TYROSINE PHOSPHATASE / CATALYTIC DOMAIN / WPD LOOP / SH2 DOMAIN
Function / homology
Function and homology information


negative regulation of humoral immune response mediated by circulating immunoglobulin / negative regulation of mast cell activation involved in immune response / negative regulation of B cell receptor signaling pathway / regulation of B cell differentiation / epididymis development / CD27 signaling pathway / negative regulation of inflammatory response to wounding / transmembrane receptor protein tyrosine phosphatase activity / phosphorylation-dependent protein binding / Co-inhibition by BTLA ...negative regulation of humoral immune response mediated by circulating immunoglobulin / negative regulation of mast cell activation involved in immune response / negative regulation of B cell receptor signaling pathway / regulation of B cell differentiation / epididymis development / CD27 signaling pathway / negative regulation of inflammatory response to wounding / transmembrane receptor protein tyrosine phosphatase activity / phosphorylation-dependent protein binding / Co-inhibition by BTLA / negative regulation of lipopolysaccharide-mediated signaling pathway / negative regulation of neutrophil activation / CD22 mediated BCR regulation / alpha-beta T cell receptor complex / regulation of release of sequestered calcium ion into cytosol / Interleukin-37 signaling / positive regulation of cell adhesion mediated by integrin / Signal regulatory protein family interactions / platelet formation / Regulation of KIT signaling / megakaryocyte development / Signaling by ALK / negative regulation of T cell receptor signaling pathway / natural killer cell mediated cytotoxicity / Platelet sensitization by LDL / regulation of type I interferon-mediated signaling pathway / PECAM1 interactions / regulation of G1/S transition of mitotic cell cycle / negative regulation of interleukin-6 production / Regulation of IFNA/IFNB signaling / peptidyl-tyrosine dephosphorylation / negative regulation of tumor necrosis factor production / Interleukin-3, Interleukin-5 and GM-CSF signaling / Co-inhibition by PD-1 / Interleukin receptor SHC signaling / negative regulation of MAPK cascade / Regulation of IFNG signaling / hematopoietic progenitor cell differentiation / Growth hormone receptor signaling / regulation of ERK1 and ERK2 cascade / T cell proliferation / Nuclear events stimulated by ALK signaling in cancer / protein dephosphorylation / GPVI-mediated activation cascade / cell adhesion molecule binding / negative regulation of T cell proliferation / T cell costimulation / phosphotyrosine residue binding / protein tyrosine phosphatase activity / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity, metal-dependent / histone H2AXY142 phosphatase activity / non-membrane spanning protein tyrosine phosphatase activity / SH2 domain binding / negative regulation of innate immune response / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / T cell activation / negative regulation of angiogenesis / B cell receptor signaling pathway / cytokine-mediated signaling pathway / peptidyl-tyrosine phosphorylation / SH3 domain binding / platelet aggregation / specific granule lumen / Interferon gamma signaling / Interferon alpha/beta signaling / MAPK cascade / tertiary granule lumen / cell-cell junction / mitotic cell cycle / T cell receptor signaling pathway / regulation of apoptotic process / cell differentiation / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / G protein-coupled receptor signaling pathway / negative regulation of cell population proliferation / positive regulation of cell population proliferation / Neutrophil degranulation / protein kinase binding / nucleolus / SARS-CoV-2 activates/modulates innate and adaptive immune responses / protein-containing complex / extracellular exosome / extracellular region / nucleoplasm / nucleus / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
: / Protein-tyrosine phosphatase, non-receptor type-6, -11 / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif ...: / Protein-tyrosine phosphatase, non-receptor type-6, -11 / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif / Tyrosine specific protein phosphatases active site. / Protein-tyrosine phosphatase, active site / Tyrosine-specific protein phosphatases domain / Tyrosine specific protein phosphatases domain profile. / Protein-tyrosine phosphatase-like / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH2 domain superfamily / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Tyrosine-protein phosphatase non-receptor type 6
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsYang, J. / Liang, X. / Niu, T. / Meng, W. / Zhao, Z. / Zhou, G.W.
Citation
Journal: J.Biol.Chem. / Year: 1998
Title: Crystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1.
Authors: Yang, J. / Liang, X. / Niu, T. / Meng, W. / Zhao, Z. / Zhou, G.W.
#1: Journal: J.Struct.Biol. / Year: 1997
Title: Expression, Purification, and Crystallization of the Catalytic Domain of Protein Tyrosine Phosphatase Shp-1
Authors: Liang, X. / Meng, W. / Niu, T. / Zhao, Z. / Zhou, G.W.
History
DepositionAug 22, 1998Processing site: BNL
Revision 1.0Aug 22, 1999Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 7, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Apr 3, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: SHP-1


Theoretical massNumber of molelcules
Total (without water)34,2901
Polymers34,2901
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)41.820, 87.780, 43.000
Angle α, β, γ (deg.)90.00, 117.40, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein SHP-1 / PROTEIN-TYROSINE PHOSPHATASE


Mass: 34289.605 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PT7-PTP1C / Production host: Escherichia coli (E. coli) / References: UniProt: P29350, protein-tyrosine-phosphatase

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.04 Å3/Da / Density % sol: 39.79 %
Crystal growpH: 7.5 / Details: pH 7.5
Crystal grow
*PLUS
Method: unknown
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
115 %PEG100001reservoir
20.1 MHEPES1reservoir

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Data collection

DiffractionMean temperature: 85 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 1.5418
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: May 1, 1997 / Details: MIRRORS
RadiationMonochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.5→50 Å / Num. obs: 8779 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Rsym value: 0.082 / Net I/σ(I): 9.3
Reflection shellResolution: 2.5→2.57 Å / Mean I/σ(I) obs: 4.1 / Rsym value: 0.313 / % possible all: 71.8
Reflection
*PLUS
Rmerge(I) obs: 0.082

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Processing

Software
NameVersionClassification
AMoREphasing
X-PLOR3.85refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PTP-1B

Resolution: 2.5→6 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 2
RfactorNum. reflection% reflectionSelection details
Rfree0.293 366 5 %RANDOM
Rwork0.209 ---
obs0.209 7392 99.7 %-
Refine analyzeLuzzati coordinate error free: 0.3 Å / Luzzati sigma a free: 0.3 Å
Refinement stepCycle: LAST / Resolution: 2.5→6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2207 0 0 0 2207
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.014
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg2.1
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d28.4
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d0.9
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
LS refinement shellResolution: 2.5→2.6 Å / Total num. of bins used: 8
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMTOPHCSDX.PRO
X-RAY DIFFRACTION2
Software
*PLUS
Name: X-PLOR / Version: 3.8.5 / Classification: refinement
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg28.4
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg0.9

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