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1oi2
From Proteopedia
(Difference between revisions)
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<StructureSection load='1oi2' size='340' side='right' caption='[[1oi2]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='1oi2' size='340' side='right' caption='[[1oi2]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1oi2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1oi2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OI2 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oi3|1oi3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oi3|1oi3]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycerone_kinase Glycerone kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.29 2.7.1.29] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycerone_kinase Glycerone kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.29 2.7.1.29] </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=1oi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oi2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1oi2 RCSB], [http://www.ebi.ac.uk/pdbsum/1oi2 PDBsum]</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=1oi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oi2 OCA], [http://pdbe.org/1oi2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oi2 RCSB], [http://www.ebi.ac.uk/pdbsum/1oi2 PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DHAK_ECOLI DHAK_ECOLI]] Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. Binds covalently dihydroxyacetone in hemiaminal linkage. Acts also as a corepressor of DhaR by binding to its sensor domain, in the absence of dihydroxyacetone. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 1oi2" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus coli migula 1895]] |
[[Category: Glycerone kinase]] | [[Category: Glycerone kinase]] | ||
[[Category: Baumann, U]] | [[Category: Baumann, U]] | ||
Revision as of 15:52, 11 September 2015
X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI
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