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. 2013 Mar 6;8(3):e58298. doi: 10.1371/journal.pone.0058298

Figure 6. Modeled structures of AstC with substrates and products.

Figure 6

6A: Shown here is AO (grey) docked into the active site of SO transaminase. Pyridoxyl phosphate is shown in magenta covalently bound to Lys 252. Hydrogen bonds between Arg 141 and AO are shown in black. This is the highest scoring pose that was correctly oriented for catalysis (6 out of 100). 6B: Shown here is the top scoring conformation of α-ketoglutarate (grey) docked into SO transaminase with pyridoxamine phosphate (magenta). Hydrogen bonds with Arg 141 are shown in black. 6C: Shown here is the top-scoring pose of SO (grey, SO-m) docked into the active site of SO transaminase. Pyridoxyl phosphate is shown in magenta covalently bound to Lys 252. Hydrogen bonds between SO and Arg 141 are shown in black. In cyan is the product succinyl-glutamic semialdehyde (SO-c, derived from the crystal structure by replacing the covalently bound amine group with the appropriate aldehyde). Hydrogen bonds from this ligand to Arg 141 are shown in cyan. In this image the docked structure (grey) has a root-mean-square distance of 1.8Å relative to the crystal structure (cyan). 6D: Shown here is glutamate (grey) docked into the active site of SO transaminase. Pyridoxyl phosphate is shown in magenta covalently bound to Lys 252. Hydrogen bonds between Arg 141 and glutamate are shown in black. This is the highest scoring pose that was correctly oriented for catalysis (2 out of 100).