4c6e

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<StructureSection load='4c6e' size='340' side='right'caption='[[4c6e]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
<StructureSection load='4c6e' size='340' side='right'caption='[[4c6e]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4c6e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C6E FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4c6e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6E FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOR:(4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC+ACID'>DOR</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NCD:N-CARBAMOYL-L-ASPARTATE'>NCD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.263&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOR:(4S)-2,6-DIOXOHEXAHYDROPYRIMIDINE-4-CARBOXYLIC+ACID'>DOR</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=NCD:N-CARBAMOYL-L-ASPARTATE'>NCD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6e OCA], [https://pdbe.org/4c6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6e RCSB], [https://www.ebi.ac.uk/pdbsum/4c6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6e ProSAT]</span></td></tr>
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<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>
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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=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>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PYR1_HUMAN PYR1_HUMAN]] This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
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[https://www.uniprot.org/uniprot/PYR1_HUMAN PYR1_HUMAN] This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4c6e" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4c6e" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[CAD protein 3D structures|CAD protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dihydroorotase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Grande-Garcia, A]]
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[[Category: Grande-Garcia A]]
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[[Category: Lallous, N]]
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[[Category: Lallous N]]
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[[Category: Ramon-Maiques, S]]
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[[Category: Ramon-Maiques S]]
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[[Category: Amidohydrolase superfamily]]
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[[Category: De novo pyrimidine biosynthesis]]
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[[Category: Histidinate anion]]
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[[Category: Hydrolase]]
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[[Category: Metalloenzyme]]
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[[Category: Zinc binding]]
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Current revision

Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 5.5

PDB ID 4c6e

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