Skip to main content
. Author manuscript; available in PMC: 2020 May 9.
Published in final edited form as: J Med Chem. 2019 Apr 30;62(9):4669–4682. doi: 10.1021/acs.jmedchem.9b00274

Figure 5.

Figure 5.

Molecular modeling of 11k and 12b. (A) Binding mode of 4c within the crystal structure of catalytic domain of humanized mouse TDP2 (PDB code: 5J4218). (B) Potential vectors for designing novel deazaflavin inhibitor types. (C) Predicted binding mode of 11k within the catalytic domain of humanized mouse TDP2. (D) Predicted binding mode of 12b within the catalytic domain of humanized mouse TDP2. Key residues are highlighted in green sticks. H-bond interactions are depicted as black dotted lines. Cation- π and π-π interaction are represented as double headed arrow in black. Water molecule and magnesium ion were represented as red and blue non-bonded sphere. All the residue numberings are based on the human TDP2.