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Figure 2.
Figure 2. A: Structural diagram of the monomeric unit of
uricase (PDB 1r51), which is also composed of a tandem
duplication of the T-fold. The N- and C-terminal domains are
colored green and gray, respectively. B: Tunnel-shaped
oligomeric complex of uricase. The active site is composed of
residues from different subunits (colored gray, beige, green,
and slate-blue) of the enzyme. The ligand molecules bound at the
active sites are shown in CPK. C: Stereo diagram of the
structure alignment of the monomeric unit of uricase and TM1553.
TM1553 is colored blue and uricase gray. Uricase does not
contain the additional helical domain. The ligands at the active
sites of uricase (shown in CPK) and TM1553 (shown as orange
spheres) are in completely different locations. D: Stereo
diagram of the putative active site of TM1553. The structure of
TM1553 is colored gray and the side-chains of residues within a
4 Å shell of the UNL are displayed in ball-and-stick
representation. The electron density of a 2Fo-Fc omit map
contoured at 1  (blue)
around the UNL (orange spheres) in the active site is shown.
Water molecules in the active site are not displayed.
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