2myu
From Proteopedia
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- | ''' | + | ==An arsenate reductase in oxidized state== |
- | + | <StructureSection load='2myu' size='340' side='right' caption='[[2myu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[2myu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MYU FirstGlance]. <br> | |
- | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2myn|2myn]], [[2myp|2myp]], [[2myt|2myt]]</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=2myu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2myu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2myu RCSB], [http://www.ebi.ac.uk/pdbsum/2myu PDBsum]</span></td></tr> | |
- | + | </table> | |
- | [[Category: | + | == Function == |
+ | [[http://www.uniprot.org/uniprot/ARSC_SYNY3 ARSC_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> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Hu, C]] | ||
[[Category: Hu, Y]] | [[Category: Hu, Y]] | ||
[[Category: Jin, C]] | [[Category: Jin, C]] | ||
- | [[Category: | + | [[Category: Alpha/beta/alpha sandwich fold]] |
+ | [[Category: Oxidoreductase]] |
Revision as of 20:08, 5 August 2015
An arsenate reductase in oxidized state
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