Image:Zinc-pong.gif

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Summary

Strange artifact when pymol made a morph between insulin in the T and the R state. Insulin forms a trimer of dimers, with two zinc atoms on the three-fold axis bound to histidines. Apparently, chain IDs of the zinc atoms were inconsistent between files, so the zinc atom is shown switching ligands. It looks like ping pong, so I called it zinc pong.

Licensing

Creative Commons Attribution-Share Alike 3.0 License CC-by-sa

Proteopedia Page Contributors and Editors (what is this?)

Karsten Theis

File history

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Date/TimeUserDimensionsFile sizeComment
(current)21:48, 13 July 2019Karsten Theis (Talk | contribs)300×256980 KBStrange artifact when pymol made a morph between insulin in the T and the R state. Insulin forms a trimer of dimers, with two zinc atoms on the three-fold axis bound to histidines. Apparently, chain IDs of the zinc atoms were inconsistent between files, s

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