 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](dw5063fig2_combined_mag.jpg)
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Figure 2
Overall structure of the binary Kif1519–375–Mg2+-ADP complex and comparison of the sequence/secondary structure of the Kif15 and Eg5 motor domains. (a) Stereo plots of the front and back view of the human Kif15 motor domain. α-Helices are coloured blue, β-strands green and loops/turns grey. The switch II cluster (α4–L12–α5) is highlighted in claret and the neck linker following the C-terminal helix α6 is shown in cyan. Mg2+-ADP is shown as a ball-and-stick model. (b) Structural and sequence alignment of the Eg5 (PDB entry 3hqd ; Parke et al., 2009  ) and Kif15 motor domains. Residue 16 of Eg5 is aligned with residue 24 of Kif15. Identical residues are coloured white on a red background and similar residues are shaded in red. The position of the ATP-binding pocket (N1–N4), the switch I and II regions and the position of the neck-linker regions are underlined in black. |
![[Figure 2]](dw5063fig2_combined.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
