2dkh
From Proteopedia
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| - | [[Image:2dkh.png|left|200px]] | ||
| - | + | ==Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni, in complex with the substrate== | |
| + | <StructureSection load='2dkh' size='340' side='right'caption='[[2dkh]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2dkh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DKH 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]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3HB:3-HYDROXYBENZOIC+ACID'>3HB</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=2dkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dkh OCA], [https://pdbe.org/2dkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dkh RCSB], [https://www.ebi.ac.uk/pdbsum/2dkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dkh ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MOBA_COMTE MOBA_COMTE] Converts 3-hydroxybenzoate (m-hydroxybenzoate), and to a lesser extent p-hydroxybenzoate, to 3,4-dihydroxybenzoate (protocatechuate). Also acts on a number of analogs of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions.<ref>PMID:18417078</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/dk/2dkh_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=2dkh ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Hydroxylases 3D structures|Hydroxylases 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | [[ | + | </StructureSection> |
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| - | == | + | |
| - | < | + | |
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[[Category: Comamonas testosteroni]] | [[Category: Comamonas testosteroni]] | ||
| - | [[Category: Fujiwara | + | [[Category: Large Structures]] |
| - | [[Category: Hiromoto | + | [[Category: Fujiwara S]] |
| - | [[Category: Hosokawa | + | [[Category: Hiromoto T]] |
| - | [[Category: Yamaguchi | + | [[Category: Hosokawa K]] |
| - | + | [[Category: Yamaguchi H]] | |
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Current revision
Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni, in complex with the substrate
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