4dy4

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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=4dy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dy4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dy4 RCSB], [http://www.ebi.ac.uk/pdbsum/4dy4 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=4dy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dy4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dy4 RCSB], [http://www.ebi.ac.uk/pdbsum/4dy4 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/WRBA_ECOK1 WRBA_ECOK1]] It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide (By similarity).
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</StructureSection>
</StructureSection>

Revision as of 05:01, 25 December 2014

High resolution structure of E.coli WrbA with FMN

4dy4, resolution 1.20Å

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