<p>The H3K4me3 residues are shown in yellow sticks and labeled in red. Residues surrounding the peptide binding pocket are shown as cartoon and sticks and are colored as in <a href="http://www.plosgenetics.org/article/info:doi/10.1371/journal.pgen.1003239#pgen-1003239-g003" target="_blank">Figure 3</a>. The H3K4me3 peptide is covered by electron density (2Fo-Fc map at 1.0σ).</p
<p>The 2Fo-Fc maps are contoured at 1.0 σ and are shown for the fragments of N helices comprising re...
<p>Domains D2 and D3 are colored as in <a href="http://www.plosone.org/article/info:doi/10.1371/jour...
<p>The molecular orientation is the same as bottom view in <a href="http://www.plosone.org/article/i...
<p><b>A–Electron density map of the bound peptide.</b> The Fo-Fc map, calculated by a simulated anne...
<p>(2Fo-Fc) electron density map contoured around the arginine ligand (2.0 σ). Arginine interacting ...
<p>The electron density map is contoured at 1.0σ level. The carboxyl product peptide ( violetpurple)...
<p>Electron-density map (coefficients 2∣<i>F</i><sub><i>obs</i></sub>∣ − ∣<i>F</i><sub><i>calc</i></...
<p>Binding sites in hGSTO1-1 for (A) GSSG and (B) the 4NPG are shown. The chemical entities and surr...
<p>The peptide (green) and LSD1 (brown) are highlighted (nitrogen atoms: blue; oxygen atoms: red). T...
<p>A) Prior to ligand modeling, positive electron density was observed in <i>F</i><sub>O</sub> – <i>...
<p>(A) Substrate binding cleft of hNtaq1. Carbon in the substrate-mimicking peptide, catalytic triad...
The ribbon diagram of the structure with Leu318-His351 displayed in stick representation is docked i...
<div><p>(A) Ribbon diagram showing peptide in yellow bound to side site of the β-appendage.</p> ...
<p>Maximal Speed Molecular Surface representations (<a href="http://www.scripps.edu/~sanner/html/msm...
<p>Hydrogen bonds between main chain peptide NH atoms (Gly37 and Arg38) and thymine oxygen atoms are...
<p>The 2Fo-Fc maps are contoured at 1.0 σ and are shown for the fragments of N helices comprising re...
<p>Domains D2 and D3 are colored as in <a href="http://www.plosone.org/article/info:doi/10.1371/jour...
<p>The molecular orientation is the same as bottom view in <a href="http://www.plosone.org/article/i...
<p><b>A–Electron density map of the bound peptide.</b> The Fo-Fc map, calculated by a simulated anne...
<p>(2Fo-Fc) electron density map contoured around the arginine ligand (2.0 σ). Arginine interacting ...
<p>The electron density map is contoured at 1.0σ level. The carboxyl product peptide ( violetpurple)...
<p>Electron-density map (coefficients 2∣<i>F</i><sub><i>obs</i></sub>∣ − ∣<i>F</i><sub><i>calc</i></...
<p>Binding sites in hGSTO1-1 for (A) GSSG and (B) the 4NPG are shown. The chemical entities and surr...
<p>The peptide (green) and LSD1 (brown) are highlighted (nitrogen atoms: blue; oxygen atoms: red). T...
<p>A) Prior to ligand modeling, positive electron density was observed in <i>F</i><sub>O</sub> – <i>...
<p>(A) Substrate binding cleft of hNtaq1. Carbon in the substrate-mimicking peptide, catalytic triad...
The ribbon diagram of the structure with Leu318-His351 displayed in stick representation is docked i...
<div><p>(A) Ribbon diagram showing peptide in yellow bound to side site of the β-appendage.</p> ...
<p>Maximal Speed Molecular Surface representations (<a href="http://www.scripps.edu/~sanner/html/msm...
<p>Hydrogen bonds between main chain peptide NH atoms (Gly37 and Arg38) and thymine oxygen atoms are...
<p>The 2Fo-Fc maps are contoured at 1.0 σ and are shown for the fragments of N helices comprising re...
<p>Domains D2 and D3 are colored as in <a href="http://www.plosone.org/article/info:doi/10.1371/jour...
<p>The molecular orientation is the same as bottom view in <a href="http://www.plosone.org/article/i...