<p>A ribbon-diagram structural representation of holo-PfRd showing the bound iron atom (orange sphere), as well as five surface lysine residue (blue sidechains; K2, K6, K28, K45, K50), seven surface aspartate residues (green sidechains; D13, D15, D18, D20, D34, D35, D53) and six surface glutamate residues (red sidechains : E14, E30, E31, E47, E49, E52).</p
Lysozyme is painted in red and mS100A6 is painted in blue. The interacting residues of lysozyme and ...
<p>(A) Superimposition of the 20 representative solution structures of holo-FldA. The FMN molecule i...
<p>(A) Topology diagram of Der f 7. The 4-stranded β-sheet is colored yellow and the 5-stranded β-sh...
<p><i>Panel a</i>. The aromatic residue cluster of holo-PfRd. Residues shown are W3 (red), Y10 (blue...
<p>(A) The protein mimics a right hand, whose thumb and fingers trap the ...
<p>(A) Ribbon representation of superimposition of apo-IsdX1 (pink) and holo-IsdX (grey). (B) Heme-b...
<p><i>Panel a.</i> Far-UV CD spectra of holo-PfRd (native) and different <i>aliphatic</i> residue su...
<p>(A) Overview of Isd–NEAT domains; the heme molecule and primary/secondary tyrosine residues on th...
<p>A: Cartoon representation of the PttTrHb model in cyan colour. The heme is shown as sticks colour...
<p>The figures representing each molecule are drawn to scale as an outline around the known structur...
<p>(A–H) The source of ferritin is indicated on the right top corner of each figure along with PDB I...
<p><b>A.</b> Ribbon diagram of the Fab fragment of the 1AF10 mAb bound to the TGEV RBD. Blue surface...
<p>The peptide (green) and LSD1 (brown) are highlighted (nitrogen atoms: blue; oxygen atoms: red). T...
Residue conservation between the heme-binding region of IsdG-like, OxdA, and Cld/Dyp/EfeB/HemQ. Ribb...
<p>FMN residue is shown in orange. (a) and (b)—along <i>a</i> and <i>c</i> axis, respectively.</p
Lysozyme is painted in red and mS100A6 is painted in blue. The interacting residues of lysozyme and ...
<p>(A) Superimposition of the 20 representative solution structures of holo-FldA. The FMN molecule i...
<p>(A) Topology diagram of Der f 7. The 4-stranded β-sheet is colored yellow and the 5-stranded β-sh...
<p><i>Panel a</i>. The aromatic residue cluster of holo-PfRd. Residues shown are W3 (red), Y10 (blue...
<p>(A) The protein mimics a right hand, whose thumb and fingers trap the ...
<p>(A) Ribbon representation of superimposition of apo-IsdX1 (pink) and holo-IsdX (grey). (B) Heme-b...
<p><i>Panel a.</i> Far-UV CD spectra of holo-PfRd (native) and different <i>aliphatic</i> residue su...
<p>(A) Overview of Isd–NEAT domains; the heme molecule and primary/secondary tyrosine residues on th...
<p>A: Cartoon representation of the PttTrHb model in cyan colour. The heme is shown as sticks colour...
<p>The figures representing each molecule are drawn to scale as an outline around the known structur...
<p>(A–H) The source of ferritin is indicated on the right top corner of each figure along with PDB I...
<p><b>A.</b> Ribbon diagram of the Fab fragment of the 1AF10 mAb bound to the TGEV RBD. Blue surface...
<p>The peptide (green) and LSD1 (brown) are highlighted (nitrogen atoms: blue; oxygen atoms: red). T...
Residue conservation between the heme-binding region of IsdG-like, OxdA, and Cld/Dyp/EfeB/HemQ. Ribb...
<p>FMN residue is shown in orange. (a) and (b)—along <i>a</i> and <i>c</i> axis, respectively.</p
Lysozyme is painted in red and mS100A6 is painted in blue. The interacting residues of lysozyme and ...
<p>(A) Superimposition of the 20 representative solution structures of holo-FldA. The FMN molecule i...
<p>(A) Topology diagram of Der f 7. The 4-stranded β-sheet is colored yellow and the 5-stranded β-sh...