<p>Residues encased in black are strictly conserved. Red stars indicate the tyrosine residues at Position I (<i>Pa</i>PabC Y92) and Position II (<i>Lp</i>PabC Y144). Triangles mark residues that are discussed in the text. Red triangles identify Lys140 and residues that interact directly with the Lys140-PLP adduct; yellow triangles mark residues that contribute to the organization of the active site or that participate in solvent mediated interactions between the protein and the cofactor.</p
<p>vRdPs are listed at the beginning of each row by the name of the virus encoding the appropriate v...
<p>(A) Sequence alignment of lysine riboswitches where gray shaded columns indicate the highly conse...
<p>Amino acid residues are aligned within 5 Å of the isoalloxazine moiety of FAD as well as at the p...
<p>PLP is shown in the same manner as <a href="http://www.plosone.org/article/info:doi/10.1371/journ...
<p>(A) Alignments of all <i>P</i>. <i>sojae</i> W/Y/L motifs. With respect to protein surface access...
<p>The alignment was created in ClustalX, and shows high conservancy in binding sites (letters in br...
<p>Sequences of N6N, N10P, N11P, IBN, and SPN are shown aligned by common spatial occupancy of resid...
<p>The position of the catalytic residues, the phosphate binding loop (P-loop) and the general acid ...
<p>The amino acid numbering at the top of the alignment is for <i>E. coli</i> YgjG. The residues inv...
<p>Red colored residues: coordinating with the polar groups of the ligand. Purple colored residues: ...
Alignment of L. major and human ATR (A) and ATM (B) protein sequences according to their secondary s...
<p>The catalytic residues, PLP-binding residues, and the mutation sites are identified with a red st...
Left column: visualization of the NS3-4A protease structure and surface of the binding pocket of wi...
<p>(A) Statistically optimal alignments between amino acids at positions 6 (blue) and 1′ (red) in PP...
<p>(<b>A</b>) The 3D structural alignment of 2QKT, 2F5Y, 1G9O, and 1BE9. The 27 residues, at the pos...
<p>vRdPs are listed at the beginning of each row by the name of the virus encoding the appropriate v...
<p>(A) Sequence alignment of lysine riboswitches where gray shaded columns indicate the highly conse...
<p>Amino acid residues are aligned within 5 Å of the isoalloxazine moiety of FAD as well as at the p...
<p>PLP is shown in the same manner as <a href="http://www.plosone.org/article/info:doi/10.1371/journ...
<p>(A) Alignments of all <i>P</i>. <i>sojae</i> W/Y/L motifs. With respect to protein surface access...
<p>The alignment was created in ClustalX, and shows high conservancy in binding sites (letters in br...
<p>Sequences of N6N, N10P, N11P, IBN, and SPN are shown aligned by common spatial occupancy of resid...
<p>The position of the catalytic residues, the phosphate binding loop (P-loop) and the general acid ...
<p>The amino acid numbering at the top of the alignment is for <i>E. coli</i> YgjG. The residues inv...
<p>Red colored residues: coordinating with the polar groups of the ligand. Purple colored residues: ...
Alignment of L. major and human ATR (A) and ATM (B) protein sequences according to their secondary s...
<p>The catalytic residues, PLP-binding residues, and the mutation sites are identified with a red st...
Left column: visualization of the NS3-4A protease structure and surface of the binding pocket of wi...
<p>(A) Statistically optimal alignments between amino acids at positions 6 (blue) and 1′ (red) in PP...
<p>(<b>A</b>) The 3D structural alignment of 2QKT, 2F5Y, 1G9O, and 1BE9. The 27 residues, at the pos...
<p>vRdPs are listed at the beginning of each row by the name of the virus encoding the appropriate v...
<p>(A) Sequence alignment of lysine riboswitches where gray shaded columns indicate the highly conse...
<p>Amino acid residues are aligned within 5 Å of the isoalloxazine moiety of FAD as well as at the p...