4hu7

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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=4hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hu7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hu7 RCSB], [http://www.ebi.ac.uk/pdbsum/4hu7 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=4hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hu7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hu7 RCSB], [http://www.ebi.ac.uk/pdbsum/4hu7 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/THIO_ECOLI THIO_ECOLI]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 22:31, 25 December 2014

E. coli thioredoxin variant with Pro76 as single proline residue

4hu7, resolution 1.40Å

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