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1j5l
From Proteopedia
(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=1j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j5l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j5l RCSB], [http://www.ebi.ac.uk/pdbsum/1j5l 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=1j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j5l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j5l RCSB], [http://www.ebi.ac.uk/pdbsum/1j5l PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MT1_HOMAM MT1_HOMAM]] Metallothioneins have a high content of cysteine residues that bind various heavy metals. The different forms of lobster metallothioneins may have different biological functions. Class I MTS in marine crustacea are involved in the sequestration of elevated levels of heavy-metal ions. Binds 6 metal ions. Known to bind cadmium. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 18:07, 25 December 2014
NMR STRUCTURE OF THE ISOLATED BETA_C DOMAIN OF LOBSTER METALLOTHIONEIN-1
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