Fig. 5: Structural differences between SLFN11wt and SLFN11S753D.
From: Phosphorylation-mediated conformational change regulates human SLFN11
a Ribbon representation of the SLFN11wt dimer (PDB: 7ZEL) with highlighted structural features (left). The second protomer is depicted as transparent. The ID-helix is depicted in dark green and the ID-region II in light green. Detailed view of the SLFN11wt helicase domain and the ID-regions (right). The position of residue S753 is indicated in purple. The hydrophobic interaction of residue F561 with the conserved SWAVDL motif (red) is shown. b Ribbon representation of SLFN11S753D illustrating the newly formed interfaces of the rotated helicase domain with ID-regions I and II, colored in dark and light green, respectively (left). The bound ATP is shown in black. Detailed view of the SLFN11S753D helicase domain and the ID-regions (right). The approximate position of mutation S753D (purple) is indicated.
