2l19

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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=2l19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l19 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l19 RCSB], [http://www.ebi.ac.uk/pdbsum/2l19 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=2l19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l19 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l19 RCSB], [http://www.ebi.ac.uk/pdbsum/2l19 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/P74313_SYNY3 P74313_SYNY3]] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 07:59, 25 December 2014

An arsenate reductase in the intermediate state

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