5ghk: Difference between revisions
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<StructureSection load='5ghk' size='340' side='right'caption='[[5ghk]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='5ghk' size='340' side='right'caption='[[5ghk]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ghk]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ghk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GHK FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ghk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ghk OCA], [https://pdbe.org/5ghk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ghk RCSB], [https://www.ebi.ac.uk/pdbsum/5ghk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ghk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ALBU_CANLF ALBU_CANLF] Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity).[UniProtKB:P02768][UniProtKB:P02769] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Canis lupus familiaris]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Akiyama | [[Category: Akiyama M]] | ||
[[Category: Kihira | [[Category: Kihira K]] | ||
[[Category: Komatsu | [[Category: Komatsu T]] | ||
[[Category: Kureishi | [[Category: Kureishi M]] | ||
[[Category: Shinohara | [[Category: Shinohara R]] | ||
[[Category: Yamada | [[Category: Yamada K]] | ||
[[Category: Yokomaku | [[Category: Yokomaku K]] | ||
