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Catalytic versatility and backups in enzyme active sites: The case of serum paraoxanase 1
Moshe Ben-David, Mikael Elias, Jean-Jacques Filippi, Elisabet Dunach, Israel Silman, Joel Sussman and Dan Tawfik, PhD[1]
Molecular Tour
Figure 2. Structural details of the 2HQ/rePON1 complex at pH 6.5; 2HQ and the
structured active-site loop in the rePON1-2HQ complex structure. Overlay of the phosphate ion in the apo rePON1 at pH 6.5 and of 2HQ
in the rePON1-2HQ complex. The first segment of the active-site loop, and residues Y71
and I74 in particular, comprises part of PON1's active-site wall. Interactions of 2HQ with
active-site residues (interactions with the catalytic Ca2+ are highlighted in red).
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rePON1 with 2HQ |
rePON1 at pH of 6.5 |
rePON1 at pH of 4.5 |
- ↑ none yet
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