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. 2012 Jul 10;13(7):8578–8596. doi: 10.3390/ijms13078578

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© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Comparison of the catalytic and enzymatically important residues (A) in camel (marine blue) and human (cyan color) APEX1 and DNA structure (orange color), and the APEX-DNA backbone interaction residues (B) in camel and human APEX1. The active sites of the cAPEX1 from the two organisms contain the highly conserved E96, N210, N212, D283, D308 and H309 residues. The residues are numbered according to the amino acid sequence of C. dromedarius (accession number ADJ96599). This comparison indicated very high identity between the predicted active site of cAPEX1 and that of hAPEX1.