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4c6e
From Proteopedia
(Difference between revisions)
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==Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 5.5== | ==Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 5.5== | ||
<StructureSection load='4c6e' size='340' side='right' caption='[[4c6e]], [[Resolution|resolution]] 1.26Å' scene=''> | <StructureSection load='4c6e' size='340' side='right' caption='[[4c6e]], [[Resolution|resolution]] 1.26Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c6b|4c6b]], [[4c6c|4c6c]], [[4c6d|4c6d]], [[4c6f|4c6f]], [[4c6i|4c6i]], [[4c6j|4c6j]], [[4c6k|4c6k]], [[4c6l|4c6l]], [[4c6m|4c6m]], [[4c6n|4c6n]], [[4c6o|4c6o]], [[4c6p|4c6p]], [[4c6q|4c6q]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c6b|4c6b]], [[4c6c|4c6c]], [[4c6d|4c6d]], [[4c6f|4c6f]], [[4c6i|4c6i]], [[4c6j|4c6j]], [[4c6k|4c6k]], [[4c6l|4c6l]], [[4c6m|4c6m]], [[4c6n|4c6n]], [[4c6o|4c6o]], [[4c6p|4c6p]], [[4c6q|4c6q]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydroorotase Dihydroorotase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.3 3.5.2.3] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydroorotase Dihydroorotase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.3 3.5.2.3] </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=4c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c6e RCSB], [http://www.ebi.ac.uk/pdbsum/4c6e 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=4c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6e OCA], [http://pdbe.org/4c6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c6e RCSB], [http://www.ebi.ac.uk/pdbsum/4c6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6e ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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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 4c6e" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:02, 4 August 2016
Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 5.5
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