4c6d

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==Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 6.0==
==Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 6.0==
<StructureSection load='4c6d' size='340' side='right' caption='[[4c6d]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='4c6d' size='340' side='right' caption='[[4c6d]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c6b|4c6b]], [[4c6c|4c6c]], [[4c6e|4c6e]], [[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]], [[4c6e|4c6e]], [[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/Gly-Xaa_carboxypeptidase Gly-Xaa carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.4 3.4.17.4] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Gly-Xaa_carboxypeptidase Gly-Xaa carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.4 3.4.17.4] </span></td></tr>
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<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=4c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c6d RCSB], [http://www.ebi.ac.uk/pdbsum/4c6d PDBsum]</span></td></tr>
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<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=4c6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6d OCA], [http://pdbe.org/4c6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c6d RCSB], [http://www.ebi.ac.uk/pdbsum/4c6d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4c6d" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 17:14, 4 August 2016

Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 6.0

4c6d, resolution 1.30Å

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