[English] 日本語
Yorodumi
- PDB-2eyv: SH2 domain of CT10-Regulated Kinase -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2eyv
TitleSH2 domain of CT10-Regulated Kinase
Componentsv-crk sarcoma virus CT10 oncogene homolog isoform a
KeywordsSIGNALING PROTEIN / SH2
Function / homology
Function and homology information


response to hepatocyte growth factor / cellular response to endothelin / helper T cell diapedesis / cerebellar neuron development / regulation of intracellular signal transduction / response to cholecystokinin / postsynaptic specialization assembly / protein phosphorylated amino acid binding / regulation of T cell migration / response to peptide ...response to hepatocyte growth factor / cellular response to endothelin / helper T cell diapedesis / cerebellar neuron development / regulation of intracellular signal transduction / response to cholecystokinin / postsynaptic specialization assembly / protein phosphorylated amino acid binding / regulation of T cell migration / response to peptide / regulation of dendrite development / positive regulation of skeletal muscle acetylcholine-gated channel clustering / negative regulation of natural killer cell mediated cytotoxicity / response to yeast / negative regulation of wound healing / reelin-mediated signaling pathway / negative regulation of cell motility / ARMS-mediated activation / protein localization to membrane / MET receptor recycling / MET activates RAP1 and RAC1 / regulation of GTPase activity / cellular response to insulin-like growth factor stimulus / establishment of cell polarity / p130Cas linkage to MAPK signaling for integrins / enzyme-linked receptor protein signaling pathway / positive regulation of smooth muscle cell migration / dendrite development / positive regulation of Rac protein signal transduction / regulation of cell adhesion mediated by integrin / ephrin receptor signaling pathway / cellular response to nitric oxide / regulation of signal transduction / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / positive regulation of substrate adhesion-dependent cell spreading / signaling adaptor activity / cellular response to transforming growth factor beta stimulus / insulin-like growth factor receptor binding / cytoskeletal protein binding / ephrin receptor binding / phosphotyrosine residue binding / Downstream signal transduction / SH2 domain binding / cell chemotaxis / protein tyrosine kinase binding / cellular response to nerve growth factor stimulus / hippocampus development / regulation of actin cytoskeleton organization / Regulation of signaling by CBL / FCGR3A-mediated phagocytosis / positive regulation of JNK cascade / neuron migration / neuromuscular junction / lipid metabolic process / response to hydrogen peroxide / Regulation of actin dynamics for phagocytic cup formation / receptor tyrosine kinase binding / cerebral cortex development / kinase binding / VEGFA-VEGFR2 Pathway / SH3 domain binding / cell migration / actin cytoskeleton / signaling receptor complex adaptor activity / regulation of cell shape / actin cytoskeleton organization / scaffold protein binding / positive regulation of cell growth / cell population proliferation / ubiquitin protein ligase binding / regulation of transcription by RNA polymerase II / protein-containing complex / extracellular exosome / membrane / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
CRK, N-terminal SH3 domain / CRK, C-terminal SH3 domain / : / Variant SH3 domain / SH2 domain / SHC Adaptor Protein / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains ...CRK, N-terminal SH3 domain / CRK, C-terminal SH3 domain / : / Variant SH3 domain / SH2 domain / SHC Adaptor Protein / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / Src homology 3 domains / SH2 domain superfamily / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
: / Adapter molecule crk
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsKobashigawa, Y. / Tanaka, S. / Inagaki, F.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2007
Title: Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK.
Authors: Kobashigawa, Y. / Sakai, M. / Naito, M. / Yokochi, M. / Kumeta, H. / Makino, Y. / Ogura, K. / Tanaka, S. / Inagaki, F.
History
DepositionNov 10, 2005Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Nov 10, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 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 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: v-crk sarcoma virus CT10 oncogene homolog isoform a


Theoretical massNumber of molelcules
Total (without water)13,7501
Polymers13,7501
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 20
RepresentativeModel #1lowest energy

-
Components

#1: Protein v-crk sarcoma virus CT10 oncogene homolog isoform a / CT10-Regulated Kinase


Mass: 13750.260 Da / Num. of mol.: 1 / Fragment: SH2 domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pPRO EX-htb / Production host: Escherichia coli (E. coli) / References: GenBank: 41327712, UniProt: P46108*PLUS

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-SEPARATED NOESY
1213D 13C-SEPARATED NOESY

-
Sample preparation

DetailsContents: 1.0MM SH2 U-15N, 13C PHOSPHATE BUFFER NA; 200MM NACL;90%H2O, 10%D2O
Sample conditionsIonic strength: 250mM / pH: 6.8 / Pressure: AMBIENT / Temperature: 298 K

-
NMR measurement

NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 800 MHz

-
Processing

NMR software
NameVersionDeveloperClassification
CYANA2Guetntert P.refinement
XEASYstructure solution
Oliviastructure solution
NMRPipestructure solution
CYANA2Guetntert P.structure solution
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformers calculated total number: 20 / Conformers submitted total number: 1

+
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://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