Sandbox 167: Difference between revisions

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The active site for 2D1S lies within a central area of the protein, and is composed of an α-helix (residues 248-260) and four short β-sheets (residues 286-289, 313-316, 339-342 and 351-353. Ile288 has been implicated as an important residue in determining the hydrophobicity of the active site environment, and through orientation of the product oxyluciferin, the bioluminescent colour. <ref name="main" />.
The active site for 2D1S lies within a central area of the protein, and is composed of an α-helix (residues 248-260) and four short β-sheets (residues 286-289, 313-316, 339-342 and 351-353. Ile288 has been implicated as an important residue in determining the hydrophobicity of the active site environment, and through orientation of the product oxyluciferin, the bioluminescent colour. <ref name="main" />.


[[Image:IMAGENAMEHERE.jpg | thumb |none | upright=3.0 | Figure 1: Caption for figure 1]]
[[Image:Image:2d1s active site with ILE288.jpg | thumb |none | upright=3.0 | Figure 1: Caption for figure 1]]


  Notes about the image
  Notes about the image

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Andrea Gorrell, James Jones