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![[Figure 3]](chr5007fig3mag.jpg)
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Figure 3
Compound 1 co-crystallized with the SER mutant PLK1K225D/K226A. (a) shows an overall view of the kinase domain of PLK1K225D/K226A (compound 1 in stick representation, C atoms in yellow). Chain A of the two PLK1 chains in the asymmetric unit is shown (PDB entry 9r1w). (b) 2Fo − Fc density map contoured at 1.3σ, with Cys133 at the hinge of PLK1 and the gatekeeper residue Leu130 shown in stick representation for orientation. (c) and (d) show a view into the ATP-binding pocket of PLK1, with PLK1 in surface representation. PLK1 residues lining the inhibitor-binding site are shown with C atoms in white and in stick representation. PLK1 is depicted with a semi-transparent surface. |
![[Figure 3]](chr5007fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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