Zinc in PDB 8qt8: Crystal Structure of Human SIRT2 in Complex with A Tnfa-Myr Analogue Tnfn-34

The structure of Crystal Structure of Human SIRT2 in Complex with A Tnfa-Myr Analogue Tnfn-34, PDB code: 8qt8 was solved by F.Friedrich, D.Kalbas, M.Meleshin, O.Einsle, M.Schutkowski, M.Jung, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.00 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	36.106, 73.339, 55.229, 90, 95.17, 90
R / Rfree (%)	18.6 / 21.2

The binding sites of Zinc atom in the Crystal Structure of Human SIRT2 in Complex with A Tnfa-Myr Analogue Tnfn-34 (pdb code 8qt8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human SIRT2 in Complex with A Tnfa-Myr Analogue Tnfn-34, PDB code: 8qt8:

Zinc binding site 1 out of 1 in the Crystal Structure of Human SIRT2 in Complex with A Tnfa-Myr Analogue Tnfn-34


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human SIRT2 in Complex with A Tnfa-Myr Analogue Tnfn-34 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:23.4 occ:1.00 SG A:CYS195 2.3 22.3 1.0 SG A:CYS224 2.3 24.6 1.0 SG A:CYS221 2.3 23.1 1.0 SG A:CYS200 2.3 27.8 1.0 CB A:CYS221 3.1 23.5 1.0 CB A:CYS200 3.1 25.0 1.0 CB A:CYS195 3.2 21.3 1.0 CB A:CYS224 3.5 25.7 1.0 N A:CYS224 3.8 25.7 1.0 CA A:CYS224 4.2 26.3 1.0 CB A:ASP223 4.4 29.9 1.0 CB A:HIS202 4.5 25.8 1.0 CA A:CYS200 4.5 26.3 1.0 CA A:CYS221 4.6 24.2 1.0 N A:ARG201 4.6 23.7 1.0 N A:HIS202 4.6 27.4 1.0 CA A:CYS195 4.6 20.7 1.0 CB A:SER226 4.7 24.6 1.0 C A:ASP223 4.7 30.7 1.0 CB A:SER197 4.7 23.7 1.0 C A:CYS224 4.8 26.6 1.0 C A:CYS200 4.8 30.0 1.0 N A:GLN225 4.9 26.4 1.0 OG A:SER226 4.9 25.2 1.0 N A:SER226 5.0 25.6 1.0 N A:ASP223 5.0 29.1 1.0 CA A:ASP223 5.0 28.2 1.0

M.Schutkowski, D.Kalbas, O.Einsle, M.Schutkowski, M.Jung. New Super-Slow Substrates As Novel Sirtuin-Inhibitors To Be Published.