7dny
From Proteopedia
(Difference between revisions)
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<StructureSection load='7dny' size='340' side='right'caption='[[7dny]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='7dny' size='340' side='right'caption='[[7dny]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[7dny]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DNY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7dny]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DNY FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HT9:coproporphyrin+III'>HT9</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HT9:coproporphyrin+III'>HT9</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7dny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dny OCA], [https://pdbe.org/7dny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dny RCSB], [https://www.ebi.ac.uk/pdbsum/7dny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dny ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7dny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dny OCA], [https://pdbe.org/7dny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dny RCSB], [https://www.ebi.ac.uk/pdbsum/7dny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dny ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [[https://www.uniprot.org/uniprot/ABCB6_HUMAN ABCB6_HUMAN]] Ocular coloboma;Dyschromatosis universalis;Colobomatous microphthalmia. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. ABCB6 mutations are involved in familial pseudohyperkalemia, a dominantly inherited condition characterized by increased serum potassium levels, measured in whole-blood specimens stored at or below room temperature. This condition is not accompanied by clinical symptoms or biological signs except for borderline abnormalities of red cell shape (PubMed:23180570).<ref>PMID:23180570</ref> | + | [[https://www.uniprot.org/uniprot/ABCB6_HUMAN ABCB6_HUMAN]] Ocular coloboma;Dyschromatosis universalis;Colobomatous microphthalmia. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. ABCB6 mutations are involved in familial pseudohyperkalemia, a dominantly inherited condition characterized by increased serum potassium levels, measured in whole-blood specimens stored at or below room temperature. This condition is not accompanied by clinical symptoms or biological signs except for borderline abnormalities of red cell shape (PubMed:23180570).<ref>PMID:23180570</ref> |
== Function == | == Function == | ||
| - | [[https://www.uniprot.org/uniprot/ABCB6_HUMAN ABCB6_HUMAN]] Binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria. Plays a crucial role in heme synthesis.<ref>PMID:10837493</ref> <ref>PMID:17006453</ref> | + | [[https://www.uniprot.org/uniprot/ABCB6_HUMAN ABCB6_HUMAN]] Binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria. Plays a crucial role in heme synthesis.<ref>PMID:10837493</ref> <ref>PMID:17006453</ref> |
<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: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hong | + | [[Category: Hong S]] |
| - | [[Category: Jin | + | [[Category: Jin MS]] |
| - | [[Category: Kang | + | [[Category: Kang JY]] |
| - | [[Category: Kim | + | [[Category: Kim JW]] |
| - | [[Category: Kim | + | [[Category: Kim NJ]] |
| - | [[Category: Kim | + | [[Category: Kim S]] |
| - | [[Category: Lee | + | [[Category: Lee SS]] |
| - | [[Category: Park | + | [[Category: Park JG]] |
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Revision as of 19:43, 7 September 2022
Cryo-EM structure of the human ABCB6 (coproporphyrin III-bound)
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Categories: Homo sapiens | Large Structures | Hong S | Jin MS | Kang JY | Kim JW | Kim NJ | Kim S | Lee SS | Park JG
