Figure 2
From: Opportunistic complexes of E. coli L-asparaginases with citrate anions
Two interpretations of the structure of Thr14 and its ligand. The mFo-DFc electron density map contoured at +3σ is shown in thin green lines. Values of ADPs of the individual atoms of ligands and those contributed by nearest residues of the enzyme are marked next to their symbols. (a) In the original structure (PDB ID 2him) Thr14 and the covalently bound L-Asp are shown in green sticks, whereas the partially overlaid L-Asn is yellow. (b) Re-interpreted structure (6nxc) is labeled in an analogous way. No residual density is present at the +3σ level. In both panels, oxygen and nitrogen atoms are colored in red and blue, respectively.
