Figure 2
From: Glutamine 89 is a key residue in the allosteric modulation of human serine racemase activity by ATP
Identification of residues involved in the formation of a H-bond network connecting the active site and the ATP binding site in SR. (A) Structural alignment of SR with bacterial threonine deaminase. The three-dimensional structure of SpSR in complex with AMP-PCP (cyan; pdb code: 1WTC) was superimposed to the three-dimensional structure of StTdcB in complex with CMP (pink; pdb code: 2GN2) using the built-in tool of Pymol. Inset reports a close up of the nucleotide binding site with PLP, nucleotide and residues forming the H-bond network shown in stick mode. Numbering is based on SpSR sequence. SpSR Q87 corresponds to Q89 in hSR sequence. (B) Logo plot of the alignment of the five amino acid residues of the H-bond network showing the reduction of uncertainty due to sequence conservation. The sequences analysed were from SR, SDH and TdcB of several organisms as detailed in Figure S1.
