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![[Figure 2]](ni5014fig2mag.jpg)
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Figure 2
Cartoon representation of the α–β plait topology of the TcNDPK1 monomer. (a) α-Helices (α1–α8) and β-sheets (β1–β4) are labeled. Important regions are highlighted: Kpn loop, orange; Head, green. The Kpn loop and Head together harbor the highly positively charged active site required for the recognition and binding of negatively charged substrates. (b) Amino acids involved in catalytic activity are shown as sticks and labeled. The most important residues are His117, which is needed for nucleotide attack, Tyr51, which plays a part in the catalytic mechanism, and Phe59, which is necessary for stacking interactions with nucleotide substrates. (c) Connolly surface and electrostatic potential calculated using APBS and PyMOL. An arrow points towards the active-site cleft. |
![[Figure 2]](ni5014fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
