5ujc

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==Crystal structure of a C.elegans B12-trafficking protein CblC, a human MMACHC homologue==
==Crystal structure of a C.elegans B12-trafficking protein CblC, a human MMACHC homologue==
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<StructureSection load='5ujc' size='340' side='right' caption='[[5ujc]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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<StructureSection load='5ujc' size='340' side='right'caption='[[5ujc]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ujc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UJC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UJC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ujc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UJC 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=COB:CO-METHYLCOBALAMIN'>COB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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]] 1.35&#8491;</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=5ujc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ujc OCA], [http://pdbe.org/5ujc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ujc RCSB], [http://www.ebi.ac.uk/pdbsum/5ujc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ujc ProSAT]</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=COB:CO-METHYLCOBALAMIN'>COB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></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=5ujc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ujc OCA], [https://pdbe.org/5ujc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ujc RCSB], [https://www.ebi.ac.uk/pdbsum/5ujc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ujc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MMAC_CAEEL MMAC_CAEEL]] Catalyzes the reductive dealkylation of cyanocobalamin to cob(II)alamin, using FAD or FMN as cofactor and NADPH as cosubstrate. Can also catalyze the glutathione-dependent reductive demethylation of methylcobalamin, and, with much lower efficiency, the glutathione-dependent reductive demethylation of adenosylcobalamin. Under anaerobic conditions cob(I)alamin is the first product; it is highly reactive and is converted to aquocob(II)alamin in the presence of oxygen. Binds cyanocobalamin, adenosylcobalamin, methylcobalamin and other, related vitamin B12 derivatives.[UniProtKB:Q9Y4U1]
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[https://www.uniprot.org/uniprot/MMAC_CAEEL MMAC_CAEEL] Catalyzes the reductive dealkylation of cyanocobalamin to cob(II)alamin, using FAD or FMN as cofactor and NADPH as cosubstrate. Can also catalyze the glutathione-dependent reductive demethylation of methylcobalamin, and, with much lower efficiency, the glutathione-dependent reductive demethylation of adenosylcobalamin. Under anaerobic conditions cob(I)alamin is the first product; it is highly reactive and is converted to aquocob(II)alamin in the presence of oxygen. Binds cyanocobalamin, adenosylcobalamin, methylcobalamin and other, related vitamin B12 derivatives.[UniProtKB:Q9Y4U1]
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Banerjee, R]]
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[[Category: Caenorhabditis elegans]]
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[[Category: Brunold, T C]]
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[[Category: Large Structures]]
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[[Category: Koutmos, M]]
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[[Category: Banerjee R]]
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[[Category: Krautler, B]]
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[[Category: Brunold TC]]
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[[Category: Lesniak, N A]]
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[[Category: Koutmos M]]
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[[Category: Li, Z]]
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[[Category: Krautler B]]
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[[Category: Ruetz, M]]
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[[Category: Lesniak NA]]
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[[Category: Shanmuganathan, A]]
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[[Category: Li Z]]
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[[Category: Yamada, K]]
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[[Category: Ruetz M]]
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[[Category: B12 binding]]
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[[Category: Shanmuganathan A]]
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[[Category: B12 processing]]
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[[Category: Yamada K]]
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[[Category: B12 trafficking]]
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[[Category: Oxidoreductase]]
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[[Category: Vitamin b12]]
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Current revision

Crystal structure of a C.elegans B12-trafficking protein CblC, a human MMACHC homologue

PDB ID 5ujc

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