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. 2024 Mar 29;7:380. doi: 10.1038/s42003-024-06078-9

Table 2.

Summary of crystal structures solved in this study

Enzyme Substrate Cofactor Resolution Treatment PDB ID
PfuSAHH SIH NAD+ 2.0 Å 22–25 °C 7R38
PfuSAHH Inosine NAD+ 2.3 Å 22–25 °C 7R37
PfuSAHH Inosine NAD+ 2.0 Å 95 °C, 15 min 8QNO
MmaSAHH Inosine NAD+ 2.5 Å 22–25 °C 7R3A
SacSAHH Adenosine NAD+ 2.6 Å 22–25 °C 7R39
MmSAHH Inosine NAD+ 2.5 Å 22–25 °C 8COD

The molecules in the asymmetric unit in all the cases were almost identical, being superimposable with a root-mean-square deviation (r.m.s.d.) of 0.17–0.63 Å over 356–393 Cα atoms. Data collection and refinement statistics are summarised in Table 3.