• DRAMP ID

    • DRAMP00748
    • Peptide Name

    • Defensin-like protein(Brazzein; Plants)
    • Source

    • Pentadiplandra brazzeana
    • Family

    • Belongs to the DEFL family
    • Gene

    • Not found
    • Sequence

    • QDKCKKVYENYPVSKCQLANQCNYDCKLDKHARSGECFYDEKRNLQCICDYCEY
    • Sequence Length

    • 54
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Antifungal
    • Target Organism

      • Gram-positive bacteria: Bacillus subtilis, Staphylococcus aureus.
      • Gram-positive bacterium: Escherichia coli.
      • Yeast: Candida albicans.
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Combine helix and strand structure
    • Structure Description

    • The brazzein fold, which contains one alpha-helix and three strands of antiparallel beta-sheet.
    • Helical Wheel Diagram

    • DRAMP00748 helical wheel diagram
    • PDB ID

    • 1BRZ resolved by NMR. 4HE7 resolved by X-ray.
  • 1BRZ-> 
    • Predicted Structure

    • There is no predicted structure for DRAMP00748.
    • Formula

    • C276H421N77O89S8
    • Absent Amino Acids

    • MTW
    • Common Amino Acids

    • CK
    • Mass

    • 6498.32
    • PI

    • 6.71
    • Basic Residues

    • 10
    • Acidic Residues

    • 9
    • Hydrophobic Residues

    • 9
    • Net Charge

    • +1
    • Boman Index

    • -155.01
    • Hydrophobicity

    • -1.106
    • Aliphatic Index

    • 43.33
    • Half Life

      • Mammalian:0.8 hour
      • Yeast:10 min
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 9440
    • Absorbance 280nm

    • 178.11
    • Polar Residues

    • 21

DRAMP00748

DRAMP00748 chydropathy plot
    • Function

    • Taste-modifying protein; sweet-tasting. It is 2000 sweeter than sucrose on a molar basis. Has a pH-specific antimicrobial activity against bacteria and fungi.
    • PTM

    • Contains four disulfide bonds 4-52; 16-37; 22-47; 26-49.
  • ·Literature 1
    • Title

    • Multidimensional signatures in antimicrobial peptides.
    • Reference

    • Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-7368.
    • Author

    • Yount NY, Yeaman MR.
  • ·Literature 2
    • Title

    • Solution structure of the thermostable sweet-tasting protein brazzein.
    • Reference

    • Nat Struct Biol. 1998 Jun;5(6):427-431.
    • Author

    • Caldwell JE, Abildgaard F, Dzakula Z, Ming D, Hellekant G, Markley JL.