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1frd
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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=1frd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1frd RCSB], [http://www.ebi.ac.uk/pdbsum/1frd 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=1frd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1frd RCSB], [http://www.ebi.ac.uk/pdbsum/1frd PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FERH_ANASP FERH_ANASP]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Donates electrons to the nitrogenase. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 09:28, 25 December 2014
MOLECULAR STRUCTURE OF THE OXIDIZED, RECOMBINANT, HETEROCYST (2FE-2S) FERREDOXIN FROM ANABAENA 7120 DETERMINED TO 1.7 ANGSTROMS RESOLUTION
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