2lhl
From Proteopedia
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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=2lhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lhl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lhl RCSB], [http://www.ebi.ac.uk/pdbsum/2lhl 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=2lhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lhl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lhl RCSB], [http://www.ebi.ac.uk/pdbsum/2lhl PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/S10A1_HUMAN S10A1_HUMAN]] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. | ||
==See Also== | ==See Also== | ||
Revision as of 20:45, 25 December 2014
Chemical Shift Assignments and solution structure of human apo-S100A1 E32Q mutant
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