 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 4]](ir5055fig4mag.jpg)
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Figure 4
Comparison of HpCNH with MtrCPA reveals conserved putrescine-binding residues. (a) The putrescine (green sticks) binding-cavity residues of both the HpCNH (gray sticks) and MtrCPA (blue sticks) structures are conserved. Also shown are residues from across the dimer interface of HpCNH (cyan sticks) and MtrCPA (black sticks). (b) Structure-based sequence alignment of HpCNH (PDB entry 6mg6) and MtrCPA (PDB entry 5h8i) structures. The secondary-structure elements are as follows: α-helices are shown as large coils, 310-helices are shown as small coils labeled η, β-strands are shown as arrows labeled β and β-turns are labeled TT. The identical residues are shown in white font on a red background, conserved residues are shown in red font and conserved regions are shown in blue boxes. (b) was generated using ESPript 3.0 (Gouet et al., 1999  , 2003). |
![[Figure 4]](ir5055fig4.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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