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5vxo
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure Analysis of human CLYBL in complex with propionyl-CoA== | |
| - | + | <StructureSection load='5vxo' size='340' side='right' caption='[[5vxo]], [[Resolution|resolution]] 2.27Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5vxo]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VXO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VXO FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1VU:PROPIONYL+COENZYME+A'>1VU</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vxc|5vxc]]</td></tr> |
| + | <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=5vxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vxo OCA], [http://pdbe.org/5vxo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vxo RCSB], [http://www.ebi.ac.uk/pdbsum/5vxo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vxo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CLYBL_HUMAN CLYBL_HUMAN]] Mitochondrial malate and beta-methylmalate synthase, which may be involved in vitamin B12 metabolism (Probable). Acts both as a malate synthase, converting glyoxylate and acetyl-CoA to malate. Also acts as a beta-methylmalate synthase by mediating conversion of glyoxylate and propionyl-CoA to beta-methylmalate (PubMed:24334609).<ref>PMID:24334609</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Shen, H]] | ||
| + | [[Category: Citrate form]] | ||
| + | [[Category: Clybl]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Peg form]] | ||
| + | [[Category: Propionyl-coa]] | ||
| + | [[Category: Trimer]] | ||
Revision as of 06:31, 1 November 2017
Crystal Structure Analysis of human CLYBL in complex with propionyl-CoA
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Categories: Shen, H | Citrate form | Clybl | Lyase | Peg form | Propionyl-coa | Trimer
