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. 2014 Oct 17;42(20):12939–12948. doi: 10.1093/nar/gku974

Figure 1.

Figure 1.

Overall structure of Oryctolagus cuniculus eEF1A2*GDP. (A) eEF1A2 is crystallized as a dimer. Three domains of eEF1A2 are colored as follows: domain I in yellow, domain II in green and domain III in blue. The Switch I and II regions are designated as S-I and S-II. The GDP is shown as a ball-and-stick representation. The N-terminus and the C-terminus are marked as Nt and Ct, respectively. (B) Presentation of the helices and beta-folds in domain I of eEF1A2*GDP. The α-helices are labeled by upper case letters, and β-strands are labeled by lower case letters. (C) Location of phosphorylated Thr239 and Ser163 in eEF1A2. (D) Network of interactions in the nucleotide-binding pocket of the GDP-bound eEF1A2. Magnesium ion is not shown for sake of clarity. (E) Electron density map corresponding to the molecule of GDP bound to eEF1A. Magnesium ion is colored in green.