1dug

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dug OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dug RCSB], [http://www.ebi.ac.uk/pdbsum/1dug PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dug OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dug RCSB], [http://www.ebi.ac.uk/pdbsum/1dug PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 06:36, 25 December 2014

STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION

1dug, resolution 1.80Å

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