Sandbox Reserved 1125: Difference between revisions
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(http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940/?page=1). The catalytic zinc ion is situated at the bottom of the active-site. The other zinc ion and the two calcium ions are packed against the top of the beta sheet and presumably function to stabilize the catalytic domain. The polypeptide folding and in particular the zinc environment of the collagenase catalytic domain bear a close ressemblance to the astacins and the snake venom metalloproteinases. | (http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940/?page=1). The catalytic zinc ion is situated at the bottom of the active-site. The other zinc ion and the two calcium ions are packed against the top of the beta sheet and presumably function to stabilize the catalytic domain. The polypeptide folding and in particular the zinc environment of the collagenase catalytic domain bear a close ressemblance to the astacins and the snake venom metalloproteinases. | ||
The catalytic domain alone has proteolytic activity against other protein substrates and synthetic substrates. | The catalytic domain alone has proteolytic activity against other protein substrates and synthetic substrates. | ||
<scene name='71/719866/S1prime_pocket/1'>S1' pocket</scene> | |||
=== Homopexin domain === | === Homopexin domain === | ||