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![[Figure 2]](jv5010fig2mag.jpg)
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Figure 2
Interatomic interactions in the stabilization loop and the active site of EcAIII. (a) Detailed view of the stabilization loop; the octahedral coordination of the sodium cation (purple sphere) is marked by dotted blue lines. (b) Residues involved in substrate/product (orange) binding in the active site (PDB entry 2zal). The oxyanion hole is formed by Gly231 (NH group) and Thr230 (OH group). (c) Stabilization of Arg207 by Glu234 and His119 in its substrate-binding position. Residues subjected to random mutagenesis are marked in cyan frames. The conserved threonine triad is comprised of Thr179 (dark blue), Thr197 and Thr230. The α subunit (chain A) is colored green, the β subunit (chain B) is colored cyan and the α subunit from the complementary dimer (chain C) is colored light pink. Hydrogen bonds are marked as red dashed lines and water molecules as red spheres. |
![[Figure 2]](jv5010fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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