journal menu
![[Figure 3]](ag5063fig3mag.jpg)
|
|
Figure 3
Structural comparisons between TANGO2 (gray, PDB entry 8sv7) and four cysteine Ntn-hydrolases. (a) Isopenicillin-N N-acyltransferase (green, PDB entry 2x1d). (b) A close-up view of the substrate-binding residues in AT (labeled in black) and their corresponding residues in TANGO2 (labeled in red). (c) Bile-salt hydrolase (cyan, PDB entry 2hf0). (d) Trp21 in BSH (labeled in black), important for substrate binding and selectivity, is replaced by Phe29 in TANGO2. (e) Acid ceramidase (brown, PDB entry 5u7z). (f) The hydrophobic substrate-binding residues of AC (labeled in black) are replaced by a short helix and Phe29 in TANGO2. (g) N-Acylethanolamine-hydrolyzing acid amidase (yellow, PDB entry 6dxx). (h) Three tryptophans in a `WWW' segment (labeled in black), important for substrate binding, are replaced by Trp83 in TANGO2. |
![[Figure 3]](ag5063fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
