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![[Figure 3]](mn9046fig3mag.jpg)
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Figure 3
Electrostatic and hydrophobic representations of the active-site tunnel of structure 1, chain A, with negatively charged residues in red and positively charged residues in blue in (a), and blue for the most polar residues to orange red for the most hydrophobic residues, and white in between (b, c and d). Generally, the active-site tunnel is polar (b, c, d). The solvent-exposed portion of loop 3 is seen as folding over at the center and composed of negatively charged residues (a). The adenine ring of ADP is at the left side of the tunnel (b) and the phosphate of AIR is at the right side of the tunnel (d). The Asp pocket, enclosed by loop 3 at the top, is polar (c). |
![[Figure 3]](mn9046fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
