Genomic structure and expression of and evolutionary analysis in the context of related JmjC domain containing proteins-5

Ve asparaginyl hydroxylase – 2636534 () and Jmjd2a (), respectively. Stereoview of the predicted structure of Jmjd6 presented as a ribbon model. The conserved eight-stranded DSBH core found in all Fe(II) and 2-oxoglutarate (2OG)-dependent dioxygenases is coloured in blue. Additional β-strands attached to the major β-sheet are shown in orange. Helices are depicted in green. View of the predicted active site of the Jmjd6-Fe(II)-2OG complex showing coordination of Fe(II) to 2OG, His187, Asp189, and His273. 2OG also ligates to Trp174, Asn197 and Lys204 with Thr285 stabilising Asn197 and Trp174. Additional important residues for putative interactions are shown in cyan and include hydrophobic interactions from Phe133 and Val275 as well as Thr184, which is involved in 2OG-binding in Hif1an. Interacting residues along with the 2OG co-substrate are shown as stick presentations, putative H-bond interactions as dotted lines. Fe(II) is depicted as an orange ball.<p><b>Copyright information:</b></p><p>Taken from "Genomic structure and expression of and evolutionary analysis in the context of related JmjC domain containing proteins"</p><p>http://www.biomedcentral.com/1471-2164/9/293</p><p>BMC Genomics 2008;9():293-293.</p><p>Published online 18 Jun 2008</p><p>PMCID:PMC2453528.</p><p>