[English] 日本語
Yorodumi
- PDB-5o2p: p130Cas SH3 domain PTP-PEST peptide chimera -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5o2p
Titlep130Cas SH3 domain PTP-PEST peptide chimera
ComponentsBreast cancer anti-estrogen resistance 1,Tyrosine-protein phosphatase non-receptor type 12
KeywordsSTRUCTURE FROM CYANA 3.97 / SH3 domain / p130Cas
Function / homology
Function and homology information


negative regulation of platelet-derived growth factor receptor-beta signaling pathway / antigen receptor-mediated signaling pathway / negative regulation of ERBB signaling pathway / regulation of epidermal growth factor receptor signaling pathway / endothelin receptor signaling pathway / tissue regeneration / Signaling by PDGF / hepatocyte growth factor receptor signaling pathway / Interleukin-37 signaling / podosome ...negative regulation of platelet-derived growth factor receptor-beta signaling pathway / antigen receptor-mediated signaling pathway / negative regulation of ERBB signaling pathway / regulation of epidermal growth factor receptor signaling pathway / endothelin receptor signaling pathway / tissue regeneration / Signaling by PDGF / hepatocyte growth factor receptor signaling pathway / Interleukin-37 signaling / podosome / cellular response to hepatocyte growth factor stimulus / p130Cas linkage to MAPK signaling for integrins / phosphoprotein phosphatase activity / neurotrophin TRK receptor signaling pathway / platelet-derived growth factor receptor signaling pathway / non-membrane spanning protein tyrosine phosphatase activity / peptidyl-tyrosine dephosphorylation / vascular endothelial growth factor receptor signaling pathway / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / cellular response to epidermal growth factor stimulus / ruffle / cell surface receptor protein tyrosine kinase signaling pathway / positive regulation of endothelial cell migration / SHC1 events in ERBB2 signaling / Downstream signal transduction / Constitutive Signaling by Overexpressed ERBB2 / protein dephosphorylation / protein-tyrosine-phosphatase / cell chemotaxis / protein tyrosine phosphatase activity / cell projection / integrin-mediated signaling pathway / regulation of cell growth / actin filament organization / EGFR downregulation / B cell receptor signaling pathway / epidermal growth factor receptor signaling pathway / Downregulation of ERBB2 signaling / VEGFA-VEGFR2 Pathway / SH3 domain binding / cell migration / actin cytoskeleton / insulin receptor signaling pathway / lamellipodium / T cell receptor signaling pathway / regulation of apoptotic process / cell adhesion / positive regulation of cell migration / G protein-coupled receptor signaling pathway / cell division / axon / focal adhesion / protein kinase binding / nucleoplasm / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Protein-tyrosine phosphatase, non-receptor type-12 / : / : / BCAR1, SH3 domain / Serine rich protein interaction domain / CAS family, C-terminal / CAS family / CAS, serine rich four helix bundle domain superfamily / Serine rich protein interaction domain / Crk-Associated Substrate C-terminal domain ...Protein-tyrosine phosphatase, non-receptor type-12 / : / : / BCAR1, SH3 domain / Serine rich protein interaction domain / CAS family, C-terminal / CAS family / CAS, serine rich four helix bundle domain superfamily / Serine rich protein interaction domain / Crk-Associated Substrate C-terminal domain / : / 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 / SH3 domain / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain
Similarity search - Domain/homology
Breast cancer anti-estrogen resistance protein 1 / Tyrosine-protein phosphatase non-receptor type 12 / Breast cancer anti-estrogen resistance 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsHexnerova, R. / Veverka, V.
CitationJournal: Sci Rep / Year: 2017
Title: Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners.
Authors: Gemperle, J. / Hexnerova, R. / Lepsik, M. / Tesina, P. / Dibus, M. / Novotny, M. / Brabek, J. / Veverka, V. / Rosel, D.
History
DepositionMay 22, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 20, 2017Provider: repository / Type: Initial release
Revision 1.1May 8, 2019Group: Data collection / Category: pdbx_nmr_software / Item: _pdbx_nmr_software.name
Revision 1.2Oct 30, 2019Group: Data collection / Database references / Category: pdbx_database_related / pdbx_nmr_spectrometer / Item: _pdbx_nmr_spectrometer.model
Revision 1.3Jun 19, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Breast cancer anti-estrogen resistance 1,Tyrosine-protein phosphatase non-receptor type 12


Theoretical massNumber of molelcules
Total (without water)10,8471
Polymers10,8471
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area0 Å2
ΔGint0 kcal/mol
Surface area7580 Å2
MethodPISA
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)40 / 100structures with the least restraint violations
RepresentativeModel #1lowest energy

-
Components

#1: Protein Breast cancer anti-estrogen resistance 1,Tyrosine-protein phosphatase non-receptor type 12 / CAS SH3 domain PTP-PEST peptide chimera / PTP-PEST / Protein-tyrosine phosphatase G1 / PTPG1 / CAS ...CAS SH3 domain PTP-PEST peptide chimera / PTP-PEST / Protein-tyrosine phosphatase G1 / PTPG1 / CAS SH3 domain PTP-PEST peptide chimera


Mass: 10847.371 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BCAR1, PTPN12 / Production host: Escherichia coli (E. coli)
References: UniProt: Q6P5Z4, UniProt: Q05209, UniProt: P56945*PLUS, protein-tyrosine-phosphatase

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic12D 1H-15N HSQC
121isotropic13D HN(CA)CB
131isotropic13D CBCA(CO)NH
141isotropic23D 1H-15N NOESY
151isotropic23D 1H-13C NOESY

-
Sample preparation

DetailsType: solution / Contents: 25 mM sodium phosphate, 1 M TCEP, 90% H2O/10% D2O / Label: 1 / Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
25 mMsodium phosphatenatural abundance1
1 MTCEPnatural abundance1
Sample conditionsIonic strength: 100 mM / Label: 1 / pH: 7.5 / Pressure: 1 atm / Temperature: 298 K

-
NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCE IIIBrukerAVANCE III6001
Bruker AVANCE IIIBrukerAVANCE III8502

-
Processing

NMR software
NameDeveloperClassification
TopSpinBruker Biospincollection
TopSpinBruker Biospinprocessing
SparkyGoddardchemical shift assignment
CYANAGuntert, Mumenthaler and Wuthrichstructure calculation
YASARAKriegerrefinement
RefinementMethod: simulated annealing / Software ordinal: 5
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 100 / Conformers submitted total number: 40

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more