 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 12]](wd5140fig12mag.jpg)
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Figure 12
Catalytic site of the mouse γ-glutamylamine cyclotransferase A2LD1. (a) Catalytic site residues of A2LD1 represented by a bundle of the five lowest-energy NMR conformers. Cyan coloring highlights residues that form hydrogen bonds with the ligands in the crystal structures. (b) Superposition of the crystal structures of A2LD1 in complex with formate (green) and human GGACT in complex with 5-oxo-L-α-proline (magenta; PDB code 3juc ; Oakley et al., 2010  ). The two structures were superimposed for best fit of the polypeptide heavy atoms shown in the drawing, yielding an r.m.s.d. of 0.62 Å. The ligands are shown inside the dotted line as yellow carbon skeletons and otherwise with standard colors for O and N atoms. The black residue numbers are for A2LD1. Owing to an insertion, the two highest residue numbers shown in the figure for GGACT are different, as indicated in magenta. |
![[Figure 12]](wd5140fig12.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
