Fig. 2: X-ray crystallography illuminates substrate recognition by DNPH1.
From: Mechanism of substrate hydrolysis by the human nucleotide pool sanitiser DNPH1
a Cartoon representation of dimeric DNPH1E104Q (chain B in yellow, chain A in light blue) bound to hmdUMP substrate (shown in sticks). A shielding loop (amino acids ~60–70, green dotted lines) is fully visualised in chain B. N- and C-termini are labelled. b Close-up view of hmdUMP bound to the active site of DNPH1E104Q chain B (yellow), supplemented by interactions from chain A (light blue). The substrate and sidechains of interacting residues are shown as sticks. The electron density for the bound ligand contoured to 2 σ is shown as a green mesh. Ligand/sidechain oxygen, nitrogen and phosphorus atoms are coloured red, blue and orange, respectively.
