6d5x

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==Structure of Human ATP:Cobalamin Adenosyltransferase bound to ATP, Adenosylcobalamin, and Triphosphate==
==Structure of Human ATP:Cobalamin Adenosyltransferase bound to ATP, Adenosylcobalamin, and Triphosphate==
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<StructureSection load='6d5x' size='340' side='right' caption='[[6d5x]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='6d5x' size='340' side='right'caption='[[6d5x]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6d5x]] is a 3 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D5X FirstGlance]. <br>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cob(I)yrinic_acid_a,c-diamide_adenosyltransferase Cob(I)yrinic acid a,c-diamide adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.17 2.5.1.17] </span></td></tr>
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<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>
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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=6d5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d5x OCA], [http://pdbe.org/6d5x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d5x RCSB], [http://www.ebi.ac.uk/pdbsum/6d5x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d5x ProSAT]</span></td></tr>
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<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>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/MMAB_HUMAN MMAB_HUMAN]] Defects in MMAB are the cause of methylmalonic aciduria type cblB (MMAB) [MIM:[http://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>
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[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>
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== Function ==
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[https://www.uniprot.org/uniprot/MMAB_HUMAN MMAB_HUMAN]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Banerjee, R]]
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[[Category: Homo sapiens]]
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[[Category: Campanello, G]]
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[[Category: Large Structures]]
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[[Category: Dodge, G J]]
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[[Category: Banerjee R]]
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[[Category: Smith, J L]]
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[[Category: Campanello G]]
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[[Category: Adenosyltransferase]]
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[[Category: Dodge GJ]]
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[[Category: B12]]
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[[Category: Smith JL]]
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[[Category: Metabolism]]
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[[Category: Transferase]]
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Current revision

Structure of Human ATP:Cobalamin Adenosyltransferase bound to ATP, Adenosylcobalamin, and Triphosphate

PDB ID 6d5x

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