 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](en5459fig3mag.jpg)
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Figure 3
(a) Cartoon representation of the crystal structure of Bh-MutT in the Mg2+-bound state (PDB entry 3hhj ). The β-strands are colored blue, α-helices red and 310-helices magenta. The 23-residue `Nudix box' consists of residues Gly42–Val64. (b) Secondary-structure diagram of Bh-MutT. The α-helices are drawn as red ovals and 310-helices as magenta ovals, with the residue number of the beginning and the end of each element shown. The β-strands are drawn as solid blue arrows with each residue indicated within a box. The β-sheets contain a bulge at residue Pro73. A solid pink line between β-strand residues indicates dual hydrogen bonds between two residues in an antiparallel β-sheet. The regions between secondary-structure elements (black lines) are not drawn to scale. |
![[Figure 3]](en5459fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
