Figure 5.
Fig. 5. Schematic view of the RING finger structures of
NOT4, IEEHV, RAG1, and c-Cbl. Please note that in RAG1, the
first zinc-binding site of the RING finger is part of the
binuclear zinc cluster. The conserved -helix is
colored red, and the remaining helices and helical turns are in
yellow. The -sheet is
colored green. Zinc ions are indicated as balls and colored
magenta for conserved zinc and gray for the remaining zinc in
RAG1. Residues that coordinate zinc ions are shown and colored
yellow for cysteine and blue for histidine.
-helix is
colored red, and the remaining helices and helical turns are in
yellow. The 
-sheet is
colored green. Zinc ions are indicated as balls and colored
magenta for conserved zinc and gray for the remaining zinc in
RAG1. Residues that coordinate zinc ions are shown and colored
yellow for cysteine and blue for histidine.