Multiple Sequence Alignment

Sequence Alignment Tables

Schematic of Cofactor Binding Sites

Graphic: Typical Catalytic Tetrad of AKRs

Graphic: Loop Structures in AKRs

Secondary Structure


Sequence Alignment Tables



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Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Multiple Sequence Alignment

Using the secondary structure of rat liver 3a-HSD (AKR1C9) as a template the positions of b-sheets, a-helices and the three large loops can be assigned.

  • B1 (82-92), B2 (94-97), H1(376-385) and H2 (438-443) are b-sheets and a-helices, respectively not in the core of the (a/b)8-barrel structure.
  • Positions of a-helices are: a1 (123-128), a2 (148-163), a3 (206-214), a4 (276-287), a5 (300-311), a6 (332-341), a7 (393-403) and a8 (423-429).
  • Positions of b-strands in the barrel are: b1 (101-104), b2 (138-140), b3 (172-175), b4 (222-225), b5 (291-295), b6 (318-326), b7 (345-349), and b8 (413-419).
  • Loop A is located from 229-272, loop B is located at 355-372 and loop C is located from 447-477.
  • Residues involved in cofactor binding are: W(104), I(140), S(298), N(199), Q(322), Y(349), K(418), S(419), I(420), R(424), and Q(427).
  • Residues involved in substrate binding are: W(104), I(144), W(229), P(230), A(366), W(367), P(457), and L(459).
  • Residues involved in catalysis are: D(140), Y(145), K(178) and H(228).
  • All residues are numbered relative to the alignments.