Template:STRUCTURE 7ahl

Hemolysin (HL) is exotoxin from bacteria which causes lysis of red blood cells.

See details for α-hemolysin in Pore forming toxin, α-hemolysin. See details of hemolysin E in Molecular Playground/ClyA.

For toxins in Proteopdia see Toxins.

3D Structures of hemolysin3D Structures of hemolysin

Updated on 29-December-2014

A full page in Proteopedia exploring 7ahl is found here.

    • 3m2l, 3m4d - SaHL-α (mutant)
    • 3m3r, 3m4e - SaHL-α (mutant) + β-cyclodextrin
    • 4idj - SaHL-α + antibody
  • β-hemolysin
    • 3k55 – SaHL-β)
    • 3i5v - SaHL-β residues 35-330)
    • 3i41 - SaHL-β residues 35-330 (mutant)
    • 3i46, 3i48 - SaHL-β residues 35-330 (mutant)
      + metal ion
  • γ-hemolysin
    • 2qk7 – SaHL-γ (mutant)
    • 3b07 - SaHL-γ
  • δ-hemolysin
    • 2kam – SaHL-δ - NMR
  • Hemolysin
    • 3o44 – VcHL residues 161-741 – Vibrio cholerae
    • 1xez – VcHL (mutant)
    • 3a57 – HL 2 – Vibrio parahaemolyticus
    • 3hvn – HL (mutant) – Streptococcus suis
    • 3fy3 – HL A residues 30-265 – Proteus mirabilis
    • 2wcd – EcHL E residues 2-303 – Escherichia coli
    • 1qoy - EcHL E (mutant)
    • 1mt0 – EcHL B ATP-binding domain
    • 2oai, 2r8d – HL corc_hlyc domain – Xylella fastidiosa
    • 2r2z – HL residues 346-435 – Enterococcus faecalis

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur, Alexander Berchansky, Michal Harel, Mark Hoelzer