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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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.