Zinc in PDB 2od2: Crystal Structure of YHST2 I117F Mutant Bound to Carba-Nad+ and An Acetylated H4 Peptide

The structure of Crystal Structure of YHST2 I117F Mutant Bound to Carba-Nad+ and An Acetylated H4 Peptide, PDB code: 2od2 was solved by B.D.Sanders, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.89 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	106.639, 106.639, 67.720, 90.00, 90.00, 120.00
R / Rfree (%)	22.5 / 23.3

The binding sites of Zinc atom in the Crystal Structure of YHST2 I117F Mutant Bound to Carba-Nad+ and An Acetylated H4 Peptide (pdb code 2od2). 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 YHST2 I117F Mutant Bound to Carba-Nad+ and An Acetylated H4 Peptide, PDB code: 2od2:

Zinc binding site 1 out of 1 in the Crystal Structure of YHST2 I117F Mutant Bound to Carba-Nad+ and An Acetylated H4 Peptide


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 YHST2 I117F Mutant Bound to Carba-Nad+ and An Acetylated H4 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:31.8 occ:1.00 SG A:CYS146 2.0 26.5 1.0 SG A:CYS170 2.4 27.9 1.0 SG A:CYS173 2.8 28.0 1.0 SG A:CYS143 2.8 29.0 1.0 CB A:CYS146 3.0 35.2 1.0 CB A:CYS143 3.2 32.1 1.0 CB A:CYS173 3.4 24.3 1.0 CB A:CYS170 3.4 23.3 1.0 N A:CYS173 3.5 31.5 1.0 N A:CYS146 3.6 33.5 1.0 CA A:CYS146 3.9 34.6 1.0 CA A:CYS173 4.0 30.5 1.0 CB A:VAL172 4.2 29.6 1.0 CB A:LYS148 4.4 29.6 1.0 CG1 A:VAL172 4.4 24.9 1.0 N A:LYS148 4.6 27.1 1.0 C A:VAL172 4.6 28.7 1.0 C A:CYS146 4.6 33.4 1.0 C A:GLY145 4.7 41.0 1.0 CA A:CYS143 4.7 30.1 1.0 N A:GLY147 4.8 35.3 1.0 CA A:VAL172 4.9 28.1 1.0 CA A:CYS170 4.9 29.1 1.0 C A:CYS173 4.9 31.0 1.0 N A:VAL172 4.9 27.1 1.0 N A:GLY174 5.0 29.9 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