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Figure 1.
Figure 1. (a) Stereo ribbon diagram of a monomer of human
estrogenic 17β-hydroxysteroid dehydrogenase (HSD). The course
of the polypeptide chain is shown for residues 1–284.
α-helices are drawn as magenta coils, β-strands as blue
arrows, and turns and loops as green ropes. The side chains for
residues in the active site belonging to the catalytic triad,
Tyr155-Lys159-Ser142, are shown in white. The view is almost
parallel to the central β-sheet. (Figure prepared using the
program SETOR [43].) (b) Folding topology of strands (triangles)
and helices (circles) in 17β-HSD. Figure 1. (a) Stereo
ribbon diagram of a monomer of human estrogenic
17β-hydroxysteroid dehydrogenase (HSD). The course of the
polypeptide chain is shown for residues 1–284. α-helices are
drawn as magenta coils, β-strands as blue arrows, and turns and
loops as green ropes. The side chains for residues in the active
site belonging to the catalytic triad, Tyr155-Lys159-Ser142, are
shown in white. The view is almost parallel to the central
β-sheet. (Figure prepared using the program SETOR [[4]43].) (b)
Folding topology of strands (triangles) and helices (circles) in
17β-HSD.
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