Skip to main content
. Author manuscript; available in PMC: 2016 Mar 3.
Published in final edited form as: Cell Rep. 2015 Feb 26;10(8):1288–1296. doi: 10.1016/j.celrep.2015.01.054

Figure 3. Structural similarities of the C6orf211 pocket with the SAM binding pocket of CheR.

Figure 3

(A) Structural superimpostions of S. cerevisiae protein YMR027W (3PT1.pdb) in cyan and S. typhimurium CheR (Uniprot code: P07801, PDB code: 1BC5.pdb) in green, revealing two acidic residues (E129 and D154 in CheR) in both proteins in similar positions within the active site. (B) Structure-based sequence alignment of human C6orf211 with S. typhimurium CheR. Conserved residues highlighted in red, stars indicate active site acidic residues, motifs I and II are highlighted with blue boxes. The first active site glutamate is conserved, the second, structurally equivalent acid residue occurs after a loop insert in C6orf211. I-Tasser predicted secondary structure shown for C6orf211 together with 1BC5.pdb secondary structure as defined by DSSP, green H indicates helix, blue E indicates strand and L is loop/coil. The conserved secondary structure elements in common with the core SAM-MT fold and the CheR insert are labeled. See also Figure S3.