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. 2003 Jan 10;100(2):455–460. doi: 10.1073/pnas.0137017100

Figure 2.

Figure 2

Catalytic site, substrate-binding pocket, and the effect of Glu-142 on catalysis. (a) Stereo view of the catalytic site of Rv2002-M3 in complex with androsterone and NADH. Glu-142 is present near the Ser-140/Tyr-153/Lys-157 catalytic triad. The final (2Fo − Fc) electron density map calculated by using 20–2.4 Å data are contoured at 1 σ for the androsterone molecule. Possible hydrogen bonds are shown as dashed lines. (b) Binding of androsterone. Three loop regions, which interact with androsterone, are shown in purple. For NADH, only the nicotinamide part is shown. (c) The effect of Glu-142 on dehydrogenase activity. The Rv2002-M3-E142A mutant recovers the dehydrogenase activity at basic pH, which is characteristic of other SDRs.