2f5i | pdb_00002f5i

X-ray structure of spermidine/spermine N1-acetyltransferase (SAT) from Homo sapiens

spinqualitylabelsall models 2f5i, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2f5i is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: Diamine N-acetyltransferase, with EC number 2.3.1.57 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [SAT1_HUMAN] Defects in SAT1 may be a cause of keratosis follicularis spinulosa decalvans X-linked (KFSDX) [MIM:308800]. A rare disorder affecting the skin and the eye. Affected men show thickening of the skin of the neck, ears, and extremities, especially the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration. Function [SAT1_HUMAN] Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine > putrescine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells. Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, N(1)-acetylspermidine and N(8)-acetylspermidine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also Spermidine/spermine N-acetyltransferase

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