 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](no5077fig1mag.jpg)
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Figure 1
Schematic representation of the primary structure of latent and active cgAUS1. The catalytically active main core is coloured red, with the copper-binding sites coloured blue, and the C-terminal domain is shown in green. Owing to a disulfide linkage of the main core to the C-terminal domain (represented by yellow connectors), the proteolytically activated enzyme possesses a remaining C-terminal peptide (Molitor et al., 2015  ). The tyrosine residue Tyr230 of active cgAUS1 is partially phosphorylated or sulfated (displayed by a violet rectangle) |
![[Figure 1]](no5077fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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