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Figure 2.
FIGURE 2. The active sites of the BphK-GSH-HOPDA ternary
complex (A) and the BphK-(GSH)[2] ternary complex (B). Residues
comprising the active site, the bound HOPDA, and the GSH
molecules are shown as ball-and-stick models. Carbon atoms are
colored yellow (GSH and HOPDA) and orange (amino acid side
chains), nitrogen atoms are colored blue, oxygen atoms are
colored red, and sulfur atoms are colored green. Secondary
structures of the two monomers comprising a homodimer are
colored in cyan and slate. Average distances are indicated
beside dotted lines. C, stereo image of the superposition of the
active sites of the BphK-GSH-HOPDA and the BphK-(GSH)[2]
complexes. Side chain carbon atoms from the BphK-GSH-HOPDA
complex are colored beige, and the GSH and HOPDA carbon atoms
are colored yellow. Side chain carbon atoms from the
BphK-(GSH)[2] complex are colored orange, and the carbon atoms
of the two GSH molecules are colored cyan. In both structures,
oxygen atoms are colored red, nitrogen atoms are colored blue,
and sulfur atoms are colored magenta.
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