2ogj
From Proteopedia
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| - | [[Image:2ogj.png|left|200px]] | ||
| - | + | ==Crystal structure of a dihydroorotase== | |
| + | <StructureSection load='2ogj' size='340' side='right'caption='[[2ogj]], [[Resolution|resolution]] 2.62Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ogj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_fabrum_str._C58 Agrobacterium fabrum str. C58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OGJ 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]] 2.62Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2ogj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ogj OCA], [https://pdbe.org/2ogj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ogj RCSB], [https://www.ebi.ac.uk/pdbsum/2ogj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ogj ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2ogj TOPSAN]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DEACT_AGRFC DEACT_AGRFC] Esterase that catalyzes the deacetylation of acetyl-(R)-mandelate (in vitro). Can also hydrolyze acetyl glycolate, but with lower efficiency. Has very low N-acetyl-D-amino acid deacetylase activity with N-acetyl-D-serine and N-acetyl-D-threonine (in vitro). Theoretical substrate docking studies suggest that other N-acetylated amino acids may optimally occupy the active site and may in fact be the physiological substrates.<ref>PMID:23214420</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[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/og/2ogj_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=2ogj ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Dihydroorotase 3D structures|Dihydroorotase 3D structures]] | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| - | [[Category: Agrobacterium | + | </StructureSection> |
| - | [[Category: | + | [[Category: Agrobacterium fabrum str. C58]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Burley SK]] |
| - | [[Category: Sugadev | + | [[Category: Kumaran D]] |
| - | [[Category: Swaminathan | + | [[Category: Sugadev R]] |
| - | + | [[Category: Swaminathan S]] | |
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Current revision
Crystal structure of a dihydroorotase
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