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4k8d

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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=4k8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k8d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k8d RCSB], [http://www.ebi.ac.uk/pdbsum/4k8d 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=4k8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k8d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k8d RCSB], [http://www.ebi.ac.uk/pdbsum/4k8d PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MERA_PSEAI MERA_PSEAI]] Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0).
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</StructureSection>
</StructureSection>

Revision as of 03:28, 25 December 2014

Crystal structure of the C558(464)A/C559(465)A double mutant of Tn501 MerA in complex with NADPH and Hg2+

4k8d, resolution 1.86Å

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