Zinc in PDB 2qqg: HST2 Bound to Adp-Hpd, Acetyllated Histone H4 and Nicotinamide

The structure of HST2 Bound to Adp-Hpd, Acetyllated Histone H4 and Nicotinamide, PDB code: 2qqg was solved by R.Marmorstein, B.Sanders, K.Zhao, J.Slama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.34 / 2.05
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	105.940, 105.940, 67.100, 90.00, 90.00, 120.00
R / Rfree (%)	21.8 / 24.5

The binding sites of Zinc atom in the HST2 Bound to Adp-Hpd, Acetyllated Histone H4 and Nicotinamide (pdb code 2qqg). 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 HST2 Bound to Adp-Hpd, Acetyllated Histone H4 and Nicotinamide, PDB code: 2qqg:

Zinc binding site 1 out of 1 in the HST2 Bound to Adp-Hpd, Acetyllated Histone H4 and Nicotinamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of HST2 Bound to Adp-Hpd, Acetyllated Histone H4 and Nicotinamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:31.3 occ:1.00 SG A:CYS170 2.3 25.5 1.0 SG A:CYS146 2.4 26.2 1.0 SG A:CYS143 2.4 22.9 1.0 SG A:CYS173 2.5 23.6 1.0 CB A:CYS143 3.1 27.0 1.0 CB A:CYS170 3.1 22.6 1.0 CB A:CYS146 3.2 30.0 1.0 CB A:CYS173 3.4 21.1 1.0 N A:CYS146 3.5 26.4 1.0 N A:CYS173 3.7 24.3 1.0 CA A:CYS146 3.9 25.5 1.0 CA A:CYS173 4.1 22.9 1.0 CB A:VAL172 4.4 24.1 1.0 C A:CYS146 4.6 31.4 1.0 C A:GLY145 4.6 37.1 1.0 CA A:CYS143 4.6 23.9 1.0 CA A:CYS170 4.6 20.5 1.0 N A:GLY147 4.6 27.6 1.0 CB A:LYS148 4.7 24.2 1.0 C A:CYS173 4.7 26.4 1.0 C A:VAL172 4.7 25.8 1.0 CG1 A:VAL172 4.7 25.7 1.0 N A:GLY174 4.7 19.8 1.0 N A:LYS148 4.8 25.2 1.0 CA A:GLY145 4.9 33.7 1.0 N A:GLY145 4.9 30.2 1.0 N A:GLU175 4.9 20.6 1.0 CA A:VAL172 5.0 25.9 1.0

B.D.Sanders, K.Zhao, J.T.Slama, R.Marmorstein. Structural Basis For Nicotinamide Inhibition and Base Exchange in SIR2 Enzymes. Mol.Cell V. 25 463 2007.
ISSN: ISSN 1097-2765
PubMed: 17289592
DOI: 10.1016/J.MOLCEL.2006.12.022