Fig. 1: Cryo-EM structure of human ASNS. | Nature Communications

Fig. 1: Cryo-EM structure of human ASNS.

From: 3D variability analysis reveals a hidden conformational change controlling ammonia transport in human asparagine synthetase

Fig. 1

a Schematic representation showing the N-terminal glutaminase (forest green), dimerization (magenta) and the C-terminal synthetase (cornflower blue) domains. The glutamine-binding (orange red) and synthetase active site (orange) are also indicated together with residues constituting the intramolecular tunnel (red). b EM map and (c) ribbon representation of human ASNS (coloring is identical to that used in (a)). d Close-up view of the dimerization motif showing residues (C, magenta; N, blue, O, red) participating in salt bridges (shown by cyan lines), and hydrophobic interactions. (A): monomer A; (B): monomer B.

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