2dvx
From Proteopedia
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| - | [[Image:2dvx.png|left|200px]] | ||
| - | + | ==Crystal Structure of 2,6-Dihydroxybenzoate Decarboxylase Complexed with inhibitor 2,3-dihydroxybenzaldehyde== | |
| - | + | <StructureSection load='2dvx' size='340' side='right'caption='[[2dvx]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2dvx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_sp._MTP-10005 Rhizobium sp. MTP-10005]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DVX 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]] 1.7Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=23A:2,3-DIHYDROXYBENZALDEHYDE'>23A</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2dvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dvx OCA], [https://pdbe.org/2dvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dvx RCSB], [https://www.ebi.ac.uk/pdbsum/2dvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dvx ProSAT]</span></td></tr> |
| - | [[2dvx]] is a 4 chain structure with sequence from [ | + | </table> |
| - | [[ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/GRDC_RHIS5 GRDC_RHIS5] Involved in the gamma-resorcylate (2,6-dihydroxybenzoate) catabolism (PubMed:15466039). Catalyzes the reversible decarboxylation of gamma-resorcylate to resorcinol (PubMed:15466039). The reaction is reversible, but equilibrium greatly favors the decarboxylation reaction (PubMed:15466039). Also catalyzes the decarboxylation of 2,3-dihydroxybenzoate to catechol, but does not act on 2,4-dihydroxybenzoate, 2,5-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3,5-dihydroxybenzoate, 2-hydroxybenzoate, or 3-hydroxybenzoate. Only resorcinol is carboxylated by the reverse reaction (PubMed:15466039).<ref>PMID:15466039</ref> |
| - | [[Category: | + | == Evolutionary Conservation == |
| - | [[Category: | + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dv/2dvx_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dvx ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rhizobium sp. MTP-10005]] | ||
| + | [[Category: Goto M]] | ||
Current revision
Crystal Structure of 2,6-Dihydroxybenzoate Decarboxylase Complexed with inhibitor 2,3-dihydroxybenzaldehyde
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