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. Author manuscript; available in PMC: 2017 Dec 1.
Published in final edited form as: Proteins. 2016 Oct 1;84(12):1797–1809. doi: 10.1002/prot.25162

Figure 1.

Figure 1

(A) Structural alignment of all existing JmjC domains bound to histone peptide. The histone peptides are marked in red. The JmjC domains are marked with other colors. The C and N terminals of the histone peptide are labeled as C and N, respectively. (B) The model of KDM5C catalytic core bound to histone peptide and enzymatic cofactors. The histone peptide backbone is shown in green and H3K4me3 is shown in red. Enzymatic cofactors Fe2+ ion and 2-oxoglutaric acid are marked with purple and yellow, respectively. The C and N terminals of the histone peptide are also labeled.