Sirtuiinien sinkkikoordinaatiokohdasta Zn finger ja Rossmannin poimusta

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4610301/
The enzymatic reaction mechanism for sirtuin-catalyzed NAD-dependent protein lysine deacetylation (Figure ​(Figure1)1) has been well understood through a series of elegant biochemical and structural studies.^20,21 The conserved catalytic core of sirtuins consists of a zinc-binding domain and a Rossmann fold domain (Figure ​(Figure11C).²²⁻²⁴ The active site lies at the interface of the two domains. It was thought that the acetyl lysine peptide binds first, followed by the binding of NAD.²⁵ Once the tertiary complex is formed, the carbonyl oxygen of the acetyl group attacks the C1′-position of the nicotinamide ribose, displacing nicotinamide and forming the alkylamidate intermediate (intermediate I, Figure ​Figure11B).²⁰ 

Etsin sinkkikoordinaatiokohtia  Pubmed sirtuiinipetidirakenteista ja löysin seuraavista.
SIRT7  (17q25.3)  Zn-Finger; 195C, 198C, 225C, 228 Z

• SIR2 superfamily of proteins includes silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel metabolite O-acetyl-ADP-ribose. Sir2 proteins, also known as sirtuins, are found in all eukaryotes and many archaea and prokaryotes and have been shown to regulate gene silencing, DNA repair, metabolic enzymes, and life span. The most-studied function, gene silencing, involves the inactivation of chromosome domains containing key regulatory genes by packaging them into a specialized chromatin structure that is inaccessible to DNA-binding proteins. The oligomerization state of Sir2 appears to be organism-dependent, sometimes occurring as a monomer and sometimes as a multimer. Also included in this superfamily is a group of uncharacterized Sir2-like proteins which lack certain key catalytic residues and conserved zinc binding cysteines.https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=294129

 SIRT6 (19p13.3) tästä en havainnut  täydellistä  (C4) sinkkisormea muistuttavaa

SIRT5 (6p23) (Peptidi 1..292 a.a.) , Zn-finger  166C, 169C, 181C, 194C.
SIRT4  (12q24.23-q24.31) (Peptidi 1..314 a.a.. Zn finger  169C, 172C, 220C,223C.
SIRT3 (11p15.5),(peptidi 1..257 a.a.)  Zn-finger 114C, 117C, 138C, 141C.
SIRT2 (19q13.2) (peptide 1..234 a.a.) Zn finger 160C,  163C, 184C, 187C
SIRT1 (10q21.3) (peptidi 1..44 a.a.) Tästä löytyy SIR2 alueesta joka katalysoi deasetylaasia,   sinkkisormi hahmo 68C, 71C, 92C, 95 C,

Rossmannin poimusta on Wikipediassa hyvä selitys. Se on yleinen monissa proteiineissa jotka sitovat  nukleotideja. tai kofaktoreja kuten FAD, NAD+ ja NADP+.
https://en.wikipedia.org/wiki/Rossmann_fold