   3.4.22.31 | More |
ananain exhibits a typical papain-like domain organization: an alpha-helix abundant L-domain comprised of residues 10-111 and 208-215, and a beta-sheet rich R-domain consisting of residues 1-9 and 112-207. In between the two domains there are two pocket-like structures, marked as pocket 1 and pocket 2. Pocket 1 is formed by the side chains of Gln19, Gly23, Trp26, Gly64, Trp180 and most importantly, the active site residues Cys25 and His157, the latter two residues essentially forming a catalytic diad. In contrast to pocket 1, which is geometrically flat and open, pocket 2 is deep and narrow, formed by the side chains of a number of hydrophobic residues, including Trp26, Trp66, Ile67, Ala132, Leu155 and Ala158 |
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