Figure 1. (a) A ribbon diagram of the SSH2-C. Secondary
structural elements (helix, orange; strand, blue; loop, grey),
which were assigned with the program PROCHECK, are labeled.
Catalytic triads (D377, C392S, and R398) and bound sulfate ion
are shown as a ball-and-stick representation. Boundaries of
secondary structural elements are 1
(b) The superpositions of seven DSP structures representing each
subfamily. A C trace
of the DSP18 is superposed with that of VHR. Worm model is in
blue for SSH2-C, orange for MKP-3 (pdb code:1mkp), green for VHR
(pdb code:1vhr), cyan for PRL-1 (pdb code:1xm2), yellow for
CDC14B (pdb code:1ohe), red for PTEN (pdb code:1d5r), and
magenta for myotubularin2 (pdb code:1m7r), respectively. The
superposition statistics against SSH2-C is 1.5/142 for MKP-3,
1.3/143 for VHR, 1.7/121 for PRL-1, 1.6/121 for CDC14B, 1.6/124
for PTEN, and 2.2/113 for Myotubularin2 where the former value
refers to rms deviations and that the latter one refers to the
number of superposed C atoms.
The position of catalytic cysteine is indicated as a grey ball.
(c) C trace
of SSH2-C is superimposed with that of the VHR. The region
cannot be aligned are colored green, whereas those of SSH2-C are
missing are colored red. The point of view is the same as Figure
1(a). (d) The sliced view of active sites for SSH2-C and VHR.
The molecular surface diagrams, which were produced using the
program VOIDOO, are drawn as a basket-weaved model. It shows
the depth and width of the active site pocket for SSH-2C and
VHR. The positions of catalytic cysteines are labeled in the