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CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN COMPLEXED WITH A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND: IMPLICATIONS FOR SH3-LIGAND INTERACTIONS
1BBZ
Primary Citation
 
 
  •   Molecular Description Hide
    Classification: Complex (transferase/peptide)
    Structure Weight: 30217.43
    Molecule: ABL TYROSINE KINASE
    Polymer: 1 Type: protein Length: 58
    Chains: A, C, E, G
    EC#: 2.7.10.2   
    Fragment: SH3 DOMAIN
    Organism: Homo sapiens
    Gene Names: Gene View for ABL1 ABL JTK7
    UniProtKB: Protein Feature View | Search PDB | P00519  
    Molecule: PEPTIDE P41
    Polymer: 2 Type: protein Length: 11
    Chains: B, D, F, H
     
  •   Structure Validation Hide

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  • MolProbity Ramachandran Plot
     

  •   Related Citations in PDB Entry (REMARK 1) Hide
     
  •   Source Hide
    Polymer: 1
    Scientific Name: Homo sapiens   Taxonomy   Common Name: Human Expression System: Escherichia coli  
    Polymer: 2
    Scientific Name: Synthetic construct   Taxonomy    
     
  •   Ligand Chemical Component Hide
    Identifier Formula Name View Interactions
    SO4
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    SO4 O4 S
    SULFATE ION
     
  •   Modified Residues Hide
    Identifier Formula Parent Type
    ACE
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    ACE C2 H4 O nonPolymer
     
  •   External Domain Annotations Hide
     
  •   Structural Biology Knowledgebase Data Hide
     
 
Data in orange boxes are gathered from external resources (when available).
 
  Biological Assembly 1       
Biological assembly 1 assigned by authors and generated by PISA (software)
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  •   Deposition Summary Hide
    Authors:   Pisabarro, M.T.,  Serrano, L.,  Wilmanns, M.

    Deposition:   1998-04-28
    Release:   1998-11-25
    Last Modified (REVDAT):   2009-02-24
     
  •   Revision History    Hide
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    2011-07-13
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  •   Experimental Details Hide
    Method:   X-RAY DIFFRACTION
    Exp. Data:
      Structure Factors
    Resolution[Å]:   1.65
    R-Value: 0.205 (obs.)
    R-Free: 0.266
    Space Group: P 21 21 21
    Unit Cell:
      Length [Å] Angles [°]
    a = 46.68 α = 90.00 
    b = 73.79 β = 90.00 
    c = 80.00 γ = 90.00