Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
Fe-Mn family superoxide dismutase
superoxide dismutases (SODs) catalyse the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. C-terminal domain is a mixed alpha/beta fold. [1]. 9878438. Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 A resolution. Knapp S, Kardinahl S, Hellgren N, Tibbelin G, Schafer G, Ladenstein R;. J Mol Biol 1999;285:689-702. (from Pfam)
Iron/manganese superoxide dismutases, alpha-hairpin domain
superoxide dismutases (SODs) catalyse the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. N-terminal domain is a long alpha antiparallel hairpin. A small fragment of YTRE_LEPBI matches well - sequencing error? [1]. 9878438. Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 A resolution. Knapp S, Kardinahl S, Hellgren N, Tibbelin G, Schafer G, Ladenstein R;. J Mol Biol 1999;285:689-702. (from Pfam)
superoxide dismutase
superoxide dismutase [Fe] eliminates superoxide radicals by catalyzing their conversion into hydrogen peroxide and oxygen
superoxide dismutase [Fe]
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on