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. Author manuscript; available in PMC: 2016 Mar 17.
Published in final edited form as: Biochemistry. 2015 Mar 2;54(10):1976–1987. doi: 10.1021/bi501547k

Figure 4. Comparison of acyl-enzyme intermediates in the active site of OXA-160.

Figure 4

Stereoview of the structures of OXA-160 V130D with ceftazidime (magenta; PDB 4X56) and aztreonam (blue; PDB 4X53) bound. To generate the structural alignment, key active site residues from OXA-160 V130D/ceftazidime (S81, S128, K218 and G220) were superposed with the same residues of OXA-24/40 K84D (yellow; PDB 3PAE) using the align function of PyMOL generating a relative mean square deviation (RMSD) of 0.174 Å. This process was repeated for OXA-160 V130D/aztreonam and OXA-24/40 K84D (RMSD, 0.321 Å).