5esd
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Crystal Structure of M. tuberculosis MenD bound to ThDP and Mn2+== | |
- | + | <StructureSection load='5esd' size='340' side='right' caption='[[5esd]], [[Resolution|resolution]] 2.25Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5esd]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ESD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ESD FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene></td></tr> | |
- | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5erx|5erx]], [[5ery|5ery]], [[5esu|5esu]], [[5eso|5eso]], [[5ess|5ess]]</td></tr> |
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid_synthase 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.9 2.2.1.9] </span></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=5esd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5esd OCA], [http://pdbe.org/5esd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5esd RCSB], [http://www.ebi.ac.uk/pdbsum/5esd PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/MEND_MYCTU MEND_MYCTU]] Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase]] | ||
+ | [[Category: Baker, E N]] | ||
+ | [[Category: Bashiri, G]] | ||
+ | [[Category: Bulloch, E M.M]] | ||
+ | [[Category: Jirgis, E N.M]] | ||
+ | [[Category: Johnston, J M]] | ||
+ | [[Category: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Menaquinone biosynthesis]] | ||
+ | [[Category: Mend]] | ||
+ | [[Category: Pyruvate oxidase family]] | ||
+ | [[Category: Thiamin-diphosphate dependent enzyme]] |
Revision as of 23:24, 23 June 2016
Crystal Structure of M. tuberculosis MenD bound to ThDP and Mn2+
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Categories: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase | Baker, E N | Bashiri, G | Bulloch, E M.M | Jirgis, E N.M | Johnston, J M | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase | Hydrolase | Menaquinone biosynthesis | Mend | Pyruvate oxidase family | Thiamin-diphosphate dependent enzyme