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Figure 3
Comparison of HpCNH with its closest structural neighbors. (a) Sausage plot generated by ENDScript. The ribbon (sausage) shows relative secondary-structural conservation compared with other nitrilase structures. The ribbon thickness reflects the level of secondary-structure similarity, with thinner ribbons indicating more conserved regions and thicker ribbons suggesting lower conservation, as determined by r.m.s.d. alignment of structures shown in Fig. 2[link]. The ribbon is colored based on sequence conservation, with red indicating identical residues. Also included is putrescine from PDB entry 5h8i, shown as yellow sticks. (b) HpCNH forms a typical nitrilase homodimer, with interaction between monomers involved in the catalytic cavity. One protomer is depicted as a surface plot, while the other is shown as a cyan cartoon. The protomer represented in the surface plot in (b) is in the same orientation as the protomer in (a). The surface plot is colored by sequence conservation, with red indicating identical residues. (c) Ribbon diagram of superposed tetramers of HpCNH (PDB entry 6mg6, gray) and MtrCPA (PDB entry 5h8i, cyan) reveals a similar overall quaternary structure.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 82| Part 3| March 2026| Pages 66-74
https://doi.org/10.1107/S2053230X26001330
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