Group:SMART:2010 Pingry SMART Team Models: Difference between revisions
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Tommie Hata (talk | contribs) |
Tommie Hata (talk | contribs) |
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(β/α)8 secondary structure features colored blue and red. | (β/α)8 secondary structure features colored blue and red. | ||
Three residues involved in NAD+ binding have backbones colored | Three residues involved in NAD+ binding have backbones colored green: E227, N276, R280. | ||
Two additional residues involved in NADP+ binding but not NAD+ binding have sidechains displayed: K274 or S275. | Two additional residues involved in NADP+ binding but not NAD+ binding have sidechains displayed but backbone uncolored: K274 or S275. | ||
Other residues involved in cofactor binding: S233, V234, W187. | Other residues involved in cofactor binding: S233, V234, W187. | ||
Loops that make a conformational change to bind NAD+ or NADP+ colored yellow. | |||
Amino terminus colored dark blue: [0,0,128]. | Amino terminus colored dark blue: [0,0,128]. | ||
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NAD+ shown in wireframe. | NAD+ shown in wireframe. | ||
'''Design script''' | '''Design script''' | ||
