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![[Figure 2]](cb5050fig2_combined_mag.jpg)
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Figure 2
Three-dimensional structure of SGSH. (a) Monomer. The approximate locations of domains 1 and 2 are shown (square brackets), with β-sheets in domain 2 labelled β2 and β3. β-Strands are shown in red, α-helices in blue and loops in yellow. Cystine bridges are shown in orange (Cys#1, 183–194; Cys#2, 481–495). The N-terminus (N) is shown as a blue ball and the C-terminus (C) as an orange ball. The formylglycine (FGly) 70 side chain is shown as a stick model in standard colours. The Ca2+ ion is shown as a grey ball. Glycosylation sites (`NAG-' followed by the asparagine residue number) are shown as green sticks. (b) Dimer. The dimer noncrystallographic symmetry axis lies vertically in the plane of the paper, with subunit centroids in the approximate paper plane on either side of it. FGly70, cystine bridges and glycosylations are shown as orange stick models. Other representations are as in Figs. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) and 2(a). (c) A short tunnel from a surface cleft leads to the active site. The inset on the left shows an enlargement of the boxed area. The two dimer subunits are shown in blue and cyan, FGly is shown as yellow spheres or sticks and glycosylations as green sticks. (d) Active site as viewed from its entry (stick models; the major interactions shown are described in the main text). |
![[Figure 2]](cb5050fig2_combined.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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