3o3m
From Proteopedia
(Difference between revisions)
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==(R)-2-Hydroxyisocaproyl-CoA Dehydratase== | |
| - | + | <StructureSection load='3o3m' size='340' side='right'caption='[[3o3m]], [[Resolution|resolution]] 1.82Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3o3m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O3M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O3M 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]] 1.82Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | '' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o3m OCA], [https://pdbe.org/3o3m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o3m RCSB], [https://www.ebi.ac.uk/pdbsum/3o3m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o3m ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HADB_CLODI HADB_CLODI] Involved in the reductive branch of L-leucine fermentation. Catalyzes the irreversible beta/alpha-elimination of water from (R)-2-hydroxyisocaproyl-CoA to yield isocaprenoyl-CoA. This beta/alpha-dehydration depends on the reductive formation of ketyl radicals on the substrate generated by injection of a single electron from the ATP-dependent activator protein HadI. The enzyme is specific for the R-isomer.<ref>PMID:15654892</ref> <ref>PMID:21366233</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Clostridioides difficile]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Buckel W]] | ||
| + | [[Category: Dobbek H]] | ||
| + | [[Category: Knauer SH]] | ||
Current revision
(R)-2-Hydroxyisocaproyl-CoA Dehydratase
| |||||||||||
