This Sandbox is Reserved from May 10, 2015, through July 31, 2015 for use by the class Protein 3D Structure Visualization & Structural Bioinformatics taught by Eric Martz and Keiichi Namba at Osaka University, Japan. This reservation includes Sandbox Reserved 1 through Sandbox Reserved 10. Syllabus.
To get started:
  • Click the 'edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Getting Started in Proteopedia, Help:Editing, Main Help Page.

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Drag the structure with the mouse to rotate

Cationic+ atoms are colored blue. 65+, including 25+ with incomplete sidechains. (21 Arg, 44 Lys) (6 His)

Anionic- atoms are colored red. 47-, including 12- with incomplete sidechains. (22 Asp, 24 Glu, 1 C terminus)


The catalytic pocket is highly conserved, while conservation of the remainder of the surface is more variable. Conserved regions of unknown function deserve investigation because they are likely to have important functions.


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

OCA, Isabel Bento, Eric Martz, Student