6d5x
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Human ATP:Cobalamin Adenosyltransferase bound to ATP, Adenosylcobalamin, and Triphosphate== | |
| - | + | <StructureSection load='6d5x' size='340' side='right'caption='[[6d5x]], [[Resolution|resolution]] 2.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6d5x]] is a 3 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=6D5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D5X FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PO:TRIPHOSPHATE'>3PO</scene>, <scene name='pdbligand=5AD:5-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6d5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d5x OCA], [https://pdbe.org/6d5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d5x RCSB], [https://www.ebi.ac.uk/pdbsum/6d5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d5x ProSAT]</span></td></tr> |
| - | [[Category: Banerjee | + | </table> |
| - | [[Category: | + | == Disease == |
| - | [[Category: | + | [https://www.uniprot.org/uniprot/MMAB_HUMAN MMAB_HUMAN] Defects in MMAB are the cause of methylmalonic aciduria type cblB (MMAB) [MIM:[https://omim.org/entry/251110 251110]; also known as methylmalonic aciduria type B or vitamin B12-responsive methylmalonicaciduria of cblB complementation type. MMAB is a disorder of methylmalonate and cobalamin metabolism due to defective synthesis of adenosylcobalamin. Inheritance is autosomal recessive.<ref>PMID:12471062</ref> <ref>PMID:12514191</ref> <ref>PMID:15781192</ref> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MMAB_HUMAN MMAB_HUMAN] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Banerjee R]] | ||
| + | [[Category: Campanello G]] | ||
| + | [[Category: Dodge GJ]] | ||
| + | [[Category: Smith JL]] | ||
Current revision
Structure of Human ATP:Cobalamin Adenosyltransferase bound to ATP, Adenosylcobalamin, and Triphosphate
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