Table 1.
Occurrence of various types of hydrogen bonds identified in two groups of proteins (Enzyme Classification, EC, 2.3 or 2.7) for three types of ligands.
Figure 1.
Cumulative distributions of donor-acceptor distances determined for various types of intermolecular hydrogen bond donor-acceptor pairs identified in complexes of proteins with non-halogenated ligands, in which the ligand is either a hydrogen bond donor (A) or acceptor (B).
Table 2.
Results of the Kruskal-Wallis (K-W) test in the analysis of the topology-dependent length of a hydrogen bond between a non-halogenated ligand (LH) and a protein: for each pair of hydrogen bond acceptor/donor pair the p-value for the null hypothesis that both distributions are identical was estimated according to the two-tailed multiple comparison.
Figure 2.
Cumulative distributions of NH•••O (blue) and O•••HN (red) intermolecular hydrogen bonds identified in protein complexes with non-halogenated (A, LH), fluorinated (B, LF) and otherwise halogenated ligands (C, LX).
See Table 2 for details.
Table 3.
Comparison of distributions of hydrogen bond lengths, calculated separately for fluorinated (LF), otherwise halogenated (LX), and non-halogenated ligands (LH), for the four most represented topologies of protein-ligand hydrogen bonds.
Figure 3.
Effect of a halogen atom on cumulative distributions determined for the four most abundant types of hydrogen bond donor-acceptor pairs: NH•••O (A), OH•••O (B), N•••HN (C), and O•••HN (D), respectively.
The distributions estimated for non-halogenated (LH), fluorinated (LF) and other halogenated ligands (LX) are presented in black, blue and green, respectively. See Table 3 for details.