5ujc
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of a C.elegans B12-trafficking protein CblC, a human MMACHC homologue== | |
- | + | <StructureSection load='5ujc' size='340' side='right' caption='[[5ujc]], [[Resolution|resolution]] 1.35Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <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> | |
- | + | </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> | |
- | [[Category: | + | <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> |
+ | </table> | ||
+ | == Function == | ||
+ | [[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] | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Banerjee, R]] | ||
+ | [[Category: Brunold, T C]] | ||
+ | [[Category: Koutmos, M]] | ||
+ | [[Category: Krautler, B]] | ||
+ | [[Category: Lesniak, N A]] | ||
+ | [[Category: Li, Z]] | ||
+ | [[Category: Ruetz, M]] | ||
+ | [[Category: Shanmuganathan, A]] | ||
+ | [[Category: Yamada, K]] | ||
+ | [[Category: B12 binding]] | ||
+ | [[Category: B12 processing]] | ||
+ | [[Category: B12 trafficking]] | ||
+ | [[Category: Oxidoreductase]] | ||
+ | [[Category: Vitamin b12]] |
Revision as of 13:11, 4 May 2017
Crystal structure of a C.elegans B12-trafficking protein CblC, a human MMACHC homologue
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