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1egr
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(Difference between revisions)
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</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=1egr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1egr RCSB], [http://www.ebi.ac.uk/pdbsum/1egr PDBsum]</span></td></tr> | </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=1egr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1egr RCSB], [http://www.ebi.ac.uk/pdbsum/1egr PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GLRX1_ECOLI GLRX1_ECOLI]] The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 03:14, 25 December 2014
SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN
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