Fig. 5: Structures of TDP1 bound to the 8-fluorosulfonyl quinolone 2e molecules (PDB code: 8UV1). | Communications Chemistry

Fig. 5: Structures of TDP1 bound to the 8-fluorosulfonyl quinolone 2e molecules (PDB code: 8UV1).

From: Targeted sulfur(VI) fluoride exchange-mediated covalent modification of a tyrosine residue in the catalytic pocket of tyrosyl-DNA phosphodiesterase 1

Fig. 5: Structures of TDP1 bound to the 8-fluorosulfonyl quinolone 2e molecules (PDB code: 8UV1).

a Illustration showing identified binding sites of 2e molecules (red spheres) to TDP1 at the catalytic site (for 2e-1, 2e-2) and crystallographic dimer packing interface (for 2e-3, 2e-4, 2e-5). b Structure of molecules of quinolone 2e-1 (carbon atoms in green) covalently bound to Y204 and interactions with the catalytic pocket. One molecule of quinolone 2e-2 (carbon atoms in green) π-π stacks with the covalently bound 2e-1. Fit of the compounds to the 2Fo-Fc electron density map (1.83 Å resolution, blue mesh, contoured at 1.0 σ level) is shown. c Structure of the TDP1 catalytic site bound to molecules of quinolone 2e-1 and 2e-2 overlaid with the coordinates of TDP1 complexed with DNA substrate (blue sticks, PDB code: 1NOP). d Structure of quinolone 2e-3 (green sticks) covalently bound to the crystal packing interface surface residue H310 on chain A (wheat). e Structure of the TDP1 crystallographic packing interface showing the quinolone 2e-4 (green sticks) covalently bound to the residue H310 on chain B (green).

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