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. 2005 Mar;71(3):1642–1647. doi: 10.1128/AEM.71.3.1642-1647.2005

FIG. 3.

FIG. 3.

(A) Crystal structure of C. tenuis XR with bound NADPH (1K8C). (B) Homology model of N. crassa XR with bound NADPH, built using the Insight II and MOE programs. The β-sheets are colored cyan to aid in the visualization of the (α/β)8 barrel. The catalytic tyrosine, lysine, and aspartate, as well as the bound cofactors and conserved histidine, are colored by atom type. The C-terminal regions involved in dimerization are colored red. Cys23 of C. tenuis XR (A) and Leu20 of N. crassa XR (B) are colored orange.