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. 2010 Jul 6;66(Pt 10):1190–1197. doi: 10.1107/S1744309110007177

Figure 1.

Figure 1

Gallery of selected protein structures determined by the JCSG (see also Figs. 5, 6 and 7). (a) Acetoacetate decarboxylase (ADC) subunit (PBD entry 3c8w). β-Strands in the double-barrel β-sheet are shown as coloured arrows; other secondary-structure elements and loops are shown as silver coils. (b) DUF1089 protein PA1994 (PDB entry 2h1t) coloured by rainbow. An ‘unswapped’ monomer is shown, a large β-sheet of which is folded into a spiral roll. (c) DUF1831 protein lp2179 (PDB entry 2iay) coloured by secondary structure: red, α-helix; yellow, β-strand; green, loop. (d) DUF1470 protein Jann2411 (PDB entry 3h0n) coloured by secondary structure, with the N-terminal subdomain coloured as in (c) and the C-terminal subdomain coloured using an alternative palette: cyan, α-helix; purple, β-strand; pink, loop. The sphere represents the zinc ion. (e) DUF1488 protein Shew3726 (PDB entry 2gpi) coloured by secondary structure, with the rare left-handed β-X-β unit coloured using an alternative palette. (f) DUF2006 protein NE1406 (PDB entry 2ich) viewed along the pseudo-twofold axis that relates its similar barrel domains. The topologically equivalent β-strands in both domains and in ADC (a) are shown in the same colour.