 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
journal menu
![[Figure 2]](ek5032fig2mag.jpg)
|
|
Figure 2
ADP-binding site of ctPrp16. The ADP molecule is sandwiched between the RecA1 (orange) and RecA2 (marine) domains (color scheme as in Fig. 1 ![[link]](../../../../../../logos/arrows/f_arr.gif){kind=small} ). C atoms are shown in orange/marine (protein) and green (ADP), N atoms are in blue, O atoms are in red, P atoms are in wheat, the Mg2+ ion is in light green and water molecules are shown as red spheres. Residues which are involved in ADP, water or Mg2+ binding are presented in ball-and-stick mode and are labeled according to the ctPrp16 sequence. Polar interactions are visualized as dashed black lines. (a) The adenine moiety is bound via π–π stacking and the ribose by hydrogen bonding. (b) The α- and β-phosphates participate intensively in hydrogen bonding. The central Mg2+ ion is coordinated by four water molecules, the Thr342 side chain and an O atom of the β-phosphate. (c) A two-dimensional ligand–protein interaction diagram (created with LigPlot+) depicting the network of interactions between the ADP molecule and the RecA1 and RecA2 domains of Prp16. |
![[Figure 2]](ek5032fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
access
