1dtz | pdb_00001dtz
From Proteopedia
STRUCTURE OF CAMEL APO-LACTOFERRIN DEMONSTRATES ITS DUAL ROLE IN SEQUESTERING AND TRANSPORTING FERRIC IONS SIMULTANEOUSLY:CRYSTAL STRUCTURE OF CAMEL APO-LACTOFERRIN AT 2.6A RESOLUTION.
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Structural highlights
FunctionTRFL_CAMDR Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate (By similarity). The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity (By similarity). Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also | ||||||||||||||||||
This page was last modified 09:53, 20 March 2024.