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 6
Validation of subpockets as plastic fragment-binding sites in esterase AX^PUR5. (a) 4,4-MDA-bound structure (PDB entry 29kx) in the presence of trapped peptide (green) or (b) 2,4-TDA degradation product (carbamate; PDB entry 29nv). (c) Superimposed structure of bound fragments in eP1, eP2 and eP3 with surrounding residues are shown: (d) 2,6-TDA (ethylene glycol; PDB entry 29oj), (e) 2,6-TDA (polypropylene; PDB entry 29oo). The 2mF_o − DF_c map at a 1.0σ contour level is shown as a blue mesh for fragments. Hydrogen bonds are shown as dashed yellow lines and water molecules are depicted as red spheres.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S2059798326010624

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