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 2
Structural overview of two different catalytic scaffolds for polyurethane degradation. (a) Overall structure of amidase U11 (PDB entry 30sd) with the catalytic triad depicted as sticks and L1–L4 shown in orange. (b) Overall structure of esterase AX^PUR5 (PDB entry 29jv) shown with the catalytic triad residues as sticks and the Lid1 and Lid2 domains shown in orange. (c, d) The catalytic triad (Ser173, cisSer149 and Lys79) along with two conserved serine residues that maintain the hydrogen-bonding network of amidase U11 (c) and the catalytic triad of AX^PUR5 (d). (e, f) Structures of the PMS-bound region in amidase U11 (PDB entry 30fo) (e) and esterase AX^PUR5 (PDB entry 29jy) (f) with surrounding residues shown as sticks. The 2mF_o − DF_c standard map at a 1.5σ contour level for PMS is depicted as a blue mesh.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S2059798326010624

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