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1b1x
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(Difference between revisions)
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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=1b1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b1x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b1x RCSB], [http://www.ebi.ac.uk/pdbsum/1b1x 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=1b1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b1x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b1x RCSB], [http://www.ebi.ac.uk/pdbsum/1b1x PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TRFL_HORSE TRFL_HORSE]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 21:51, 24 December 2014
STRUCTURE OF DIFERRIC MARE LACTOFERRIN AT 2.62A RESOLUTION
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