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. Author manuscript; available in PMC: 2007 Sep 7.
Published in final edited form as: J Steroid Biochem Mol Biol. 2006 Aug 4;101(1):50–60. doi: 10.1016/j.jsbmb.2006.06.004

Fig. 2.

Fig. 2

The 3D amino acid sequence alignment of 3β-HSD_1 with corresponding constituent parts of UDPGE and 17β-HSD_1. The experimental (X-ray) and predicted (PHD method [16]) secondary structure elements are indicated along the sequence The sequences and individual numbering of 3β-HSD_1, UDPGE and 17β-HSD_1 are shown in black, blue and green respectively. The yellow color marks the region, deletion of which does not cause the loss of enzyme activity.

Other indicative symbols:

#(in magenta) - oxidoreductase catalytic residues, Ser124, Tyr154, Lys158

^ (in blue) - residues lining the NAD binding shell

x (in magenta) – residues lining the substrate binding shell

$ (in magenta) – proposed 3D structure based isomerase catalytic (Glu126) and substrate recognition/binding (His232, Asn323) residues in the active site.