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- PDB-1v3a: Structure of human PRL-3, the phosphatase associated with cancer ... -

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Basic information

Entry
Database: PDB / ID: 1v3a
TitleStructure of human PRL-3, the phosphatase associated with cancer metastasis
Componentsprotein tyrosine phosphatase type IVA
KeywordsHYDROLASE
Function / homology
Function and homology information


regulation of vascular endothelial growth factor signaling pathway / prenylated protein tyrosine phosphatase activity / positive regulation of establishment of protein localization / positive regulation of vascular permeability / endothelial cell migration / dephosphorylation / Notch signaling pathway / cellular response to leukemia inhibitory factor / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity ...regulation of vascular endothelial growth factor signaling pathway / prenylated protein tyrosine phosphatase activity / positive regulation of establishment of protein localization / positive regulation of vascular permeability / endothelial cell migration / dephosphorylation / Notch signaling pathway / cellular response to leukemia inhibitory factor / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / positive regulation of non-canonical NF-kappaB signal transduction / early endosome / regulation of DNA-templated transcription / nucleus / plasma membrane / cytoplasm
Similarity search - Function
Dual specificity protein phosphatase domain / Dual specificity protein phosphatase domain profile. / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif / Tyrosine-specific protein phosphatases domain / Tyrosine specific protein phosphatases domain profile. ...Dual specificity protein phosphatase domain / Dual specificity protein phosphatase domain profile. / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif / Tyrosine-specific protein phosphatases domain / Tyrosine specific protein phosphatases domain profile. / Protein-tyrosine phosphatase-like / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Protein tyrosine phosphatase type IVA 3
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
Model type detailsminimized average
AuthorsJeon, Y.H. / Cheong, C.
CitationJournal: Febs Lett. / Year: 2004
Title: Structure of human PRL-3, the phosphatase associated with cancer metastasis
Authors: Kim, K.A. / Song, J.S. / Jee, J. / Sheen, M.R. / Lee, C. / Lee, T.G. / Ro, S. / Cho, J.M. / Lee, W. / Yamazaki, T. / Jeon, Y.H. / Cheong, C.
History
DepositionOct 30, 2003Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 30, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: protein tyrosine phosphatase type IVA


Theoretical massNumber of molelcules
Total (without water)19,5671
Polymers19,5671
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representativeminimized average structure

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Components

#1: Protein protein tyrosine phosphatase type IVA / phosphatase


Mass: 19566.895 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET21b / Production host: Escherichia coli (E. coli) / References: UniProt: O75365, protein-tyrosine-phosphatase

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX6001
Varian UNITYVarianUNITY6002

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Processing

NMR softwareName: Amber / Classification: refinement
NMR representativeSelection criteria: minimized average structure
NMR ensembleConformers submitted total number: 1

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