Table 2.
Cluster | Subcluster | Types of ligands | Main feature |
A | I | Metal ions | Single rigid α helix connects the two domains |
II | Siderophores | ||
B | Carbohydrates, Leu, Ile, Val, autoinducer-2 | Three interconnecting segments between the two domains | |
C | Di- and oligopeptides, Arg, cellubiose, nickel | An additional domain. These SBPs are significantly larger. | |
D | I | Carbohydrates | Two relative short hinges between the two domains |
II | Putrescine, thiamine | ||
III | Tetrahedral oxyanions | ||
E | Sialic acid, 2-keto acids, ectoine, pyroglutamic acid | Large flexible helix in between the two domains. Only associated with TRAP transporters. | |
F | I | Trigonal planar anions, unknown ligands | Two hinges in between the two domains as in cluster D, but these hinges are almost twice as long, giving the SBP more flexibility |
II | Methionine | ||
III | Compatible solutes | ||
IV | Amino acids |
Data taken from Berntsson et al. (2010).