Crystal structure of c-Cbl-TKB domain complexed with its binding motif in Sprouty4
3BUN
Primary Citation
 
 
  •   Molecular Description Hide
    Classification: Ligase/signaling Protein
    Structure Weight: 39776.04
    Molecule: 13-meric peptide from Portein sprouty homolog 4
    Polymer: 1 Type: protein Length: 13
    Chains: A
    Fragment: UNP residues 46-58, pTyr-53 phosphopeptide
    Organism: Homo sapiens
    Gene Name: Gene View for SPRY4
    UniProtKB: Protein Feature View | Search PDB | Q9C004  
    Molecule: E3 ubiquitin-protein ligase CBL
    Polymer: 2 Type: protein Length: 329
    Chains: B
    EC#: 6.3.2   
    Fragment: c-Cbl TKB domain, CBL N-terminal, UNP residues 23-351
    Organism: Homo sapiens
    Gene Names: Gene View for CBL CBL2 RNF55
    UniProtKB: Protein Feature View | Search PDB | P22681  
     
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  •   Related Citations in PDB Entry (REMARK 1) Hide
     
  •   Source Hide
    Polymer: 1
    Scientific Name: Synthetic construct (Homo sapiens)   Taxonomy    
    Polymer: 2
    Scientific Name: Homo sapiens   Taxonomy   Common Name: Human Expression System: Escherichia coli  
     
  •   Related PDB Entries Hide
    Identifier Details
    3BUM   c-Cbl-TKB domain complexed with its binding motif in Sprouty2 
    3BUO   c-Cbl-TKB domain complexed with its binding motif in EGF receptor 
    3BUW   c-Cbl-TKB domain complexed with its binding motif in Syk 
    3BUX   c-Cbl-TKB domain complexed with its binding motif in c-Met 
     
  •   Modified Residues Hide
    Identifier Formula Parent Type
    PTR
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    PTR C9 H12 N O6 P TYR lPeptideLinking
     
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Data in orange boxes are gathered from external resources (when available).
  Biological Assembly 1       
Biological assembly 1 assigned by authors
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  •   Deposition Summary Hide
    Authors:   Ng, C.,  Jackson, R.A.,  Buschdorf, J.P.,  Sun, Q.,  Guy, G.R.,  Sivaraman, J.

    Deposition:   2008-01-03
    Release:   2008-02-26
    Last Modified (REVDAT):   2009-02-24
     
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    2011-07-13
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  •   Experimental Details Hide
    Method:   X-RAY DIFFRACTION
    Exp. Data:
      Structure Factors
    EDS  
    Resolution[Å]:   2.00
    R-Value: 0.201 (work)
    R-Free: 0.242
    Space Group: P 6
    Unit Cell:
      Length [Å] Angles [°]
    a = 122.85 α = 90.00 
    b = 122.85 β = 90.00 
    c = 55.54 γ = 120.00