Fragment-based active-site exploration of urethane hydrolases reveals a diversity of urethane binding modes

Bicer, D.; Kochubei, D.; Graham, R.; Peña-Díaz, S.; Rotilio, L.; Villadsen, N.L.; Sommerfeldt, A.; Johansen, M.B.; Sandahl, A.; Thirup, S.S.; Morth, J.P.; Otzen, D.E.

doi:10.1107/S2059798326010624

Figure 7
MUE-MDA and MUE-2,4-TDA transition-state analogues bound to amidase U11 and esterase AX^PUR5. (a) U11 bound to the MUE-MDA TS analog in pose 1 (PDB entry 30ge). (c) U11 bound to the MUE-MDA TS analog in pose 2 (PDB entry 30gv). (e) U11 bound to the MUE-2,4-TDA TS analog (PDB entry 30tu). (b) Esterase AX^PUR5 bound to the leaving group p-nitrophenol (PDB entry 29nw). (d) Esterase AX^PUR5 bound to the MUE-MDA TS analog (PDB entry 30tv). (f) Esterase AX^PUR5 bound to the MUE-2,4-TDA TS analog (PDB entry 30va). 2mF_o − DF_c standard maps at a 1.0σ contour level are shown for fragments as a blue mesh.

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ISSN: 2059-7983

Volume 82| Part 11| November 2026| Pages 1298-1317

https://doi.org/10.1107/S2059798326010624

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