4c6b

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:04, 20 December 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.==
==Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.==
-
<StructureSection load='4c6b' size='340' side='right' caption='[[4c6b]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
+
<StructureSection load='4c6b' size='340' side='right'caption='[[4c6b]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4c6b]] 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=4C6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C6B FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4c6b]] 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=4C6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6B FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.656&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c6c|4c6c]], [[4c6d|4c6d]], [[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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4c6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6b OCA], [https://pdbe.org/4c6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6b RCSB], [https://www.ebi.ac.uk/pdbsum/4c6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6b ProSAT]</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=4c6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6b OCA], [http://pdbe.org/4c6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c6b RCSB], [http://www.ebi.ac.uk/pdbsum/4c6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6b ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[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).
+
[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 ==
Line 20: Line 19:
</div>
</div>
<div class="pdbe-citations 4c6b" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4c6b" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[CAD protein 3D structures|CAD protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Dihydroorotase]]
+
[[Category: Homo sapiens]]
-
[[Category: Human]]
+
[[Category: Large Structures]]
-
[[Category: Grande-Garcia, A]]
+
[[Category: Grande-Garcia A]]
-
[[Category: Lallous, N]]
+
[[Category: Lallous N]]
-
[[Category: Ramon-Maiques, S]]
+
[[Category: Ramon-Maiques S]]
-
[[Category: Amidohydrolase superfamily]]
+
-
[[Category: De novo pyrimidine biosynthesis]]
+
-
[[Category: Histidinate anion]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Metalloenzyme]]
+
-
[[Category: Zinc binding]]
+

Current revision

Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.

PDB ID 4c6b

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools