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Yorodumi- PDB-1csk: THE CRYSTAL STRUCTURE OF HUMAN CSKSH3: STRUCTURAL DIVERSITY NEAR ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1csk | ||||||
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Title | THE CRYSTAL STRUCTURE OF HUMAN CSKSH3: STRUCTURAL DIVERSITY NEAR THE RT-SRC AND N-SRC LOOP | ||||||
Components | C-SRC SH3 DOMAIN | ||||||
Keywords | PHOSPHOTRANSFERASE | ||||||
Function / homology | Function and homology information negative regulation of Golgi to plasma membrane protein transport / regulation of Fc receptor mediated stimulatory signaling pathway / negative regulation of low-density lipoprotein particle clearance / proline-rich region binding / negative regulation of bone resorption / adherens junction organization / negative regulation of phagocytosis / cellular response to peptide hormone stimulus / Phosphorylation of CD3 and TCR zeta chains / oligodendrocyte differentiation ...negative regulation of Golgi to plasma membrane protein transport / regulation of Fc receptor mediated stimulatory signaling pathway / negative regulation of low-density lipoprotein particle clearance / proline-rich region binding / negative regulation of bone resorption / adherens junction organization / negative regulation of phagocytosis / cellular response to peptide hormone stimulus / Phosphorylation of CD3 and TCR zeta chains / oligodendrocyte differentiation / protein kinase A catalytic subunit binding / negative regulation of interleukin-6 production / RHOH GTPase cycle / PD-1 signaling / GAB1 signalosome / Negative regulation of FLT3 / T cell costimulation / Integrin signaling / protein tyrosine kinase binding / non-specific protein-tyrosine kinase / Signaling by high-kinase activity BRAF mutants / non-membrane spanning protein tyrosine kinase activity / MAP2K and MAPK activation / negative regulation of ERK1 and ERK2 cascade / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Signaling by BRAF and RAF1 fusions / cell-cell junction / T cell receptor signaling pathway / protein phosphatase binding / protein tyrosine kinase activity / adaptive immune response / negative regulation of cell population proliferation / protein phosphorylation / extracellular exosome / ATP binding / identical protein binding / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Mathieu, M. / Wierenga, R.K. | ||||||
Citation | Journal: FEBS Lett. / Year: 1994 Title: The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop. Authors: Borchert, T.V. / Mathieu, M. / Zeelen, J.P. / Courtneidge, S.A. / Wierenga, R.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1csk.cif.gz | 54.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1csk.ent.gz | 41 KB | Display | PDB format |
PDBx/mmJSON format | 1csk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1csk_validation.pdf.gz | 381.5 KB | Display | wwPDB validaton report |
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Full document | 1csk_full_validation.pdf.gz | 389.3 KB | Display | |
Data in XML | 1csk_validation.xml.gz | 6.3 KB | Display | |
Data in CIF | 1csk_validation.cif.gz | 9.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cs/1csk ftp://data.pdbj.org/pub/pdb/validation_reports/cs/1csk | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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4 |
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Unit cell |
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Details | THE FOUR MOLECULES ARE PACKED IN THE CELL AS A DIMER OF DIMERS, ONE DIMER BEING FORMED OF MOLECULES D AND A, AND THE OTHER OF MOLECULES B AND C. |
-Components
#1: Protein | Mass: 7851.946 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P41240, EC: 2.7.1.112 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 48.98 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: microdialysis | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 25 Å / Num. obs: 10807 / % possible obs: 94.8 % / Num. measured all: 60252 / Rmerge(I) obs: 0.083 |
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-Processing
Software |
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Refinement | Resolution: 2.5→8 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 9913 / Rfactor Rfree: 0.278 / Rfactor Rwork: 0.224 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.9 |