6ce1: Difference between revisions

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<StructureSection load='6ce1' size='340' side='right'caption='[[6ce1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='6ce1' size='340' side='right'caption='[[6ce1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ce1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CE1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ce1]] 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=6CE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CE1 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PADI3, PAD3, PDI3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.8&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-arginine_deiminase Protein-arginine deiminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.15 3.5.3.15] </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=6ce1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ce1 OCA], [https://pdbe.org/6ce1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ce1 RCSB], [https://www.ebi.ac.uk/pdbsum/6ce1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ce1 ProSAT]</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=6ce1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ce1 OCA], [https://pdbe.org/6ce1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ce1 RCSB], [https://www.ebi.ac.uk/pdbsum/6ce1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ce1 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[https://www.uniprot.org/uniprot/PADI3_HUMAN PADI3_HUMAN]] Uncombable hair syndrome. The disease is caused by mutations affecting the gene represented in this entry.  
[https://www.uniprot.org/uniprot/PADI3_HUMAN PADI3_HUMAN] Uncombable hair syndrome. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PADI3_HUMAN PADI3_HUMAN]] Catalyzes the deimination of arginine residues of proteins.<ref>PMID:27866708</ref>
[https://www.uniprot.org/uniprot/PADI3_HUMAN PADI3_HUMAN] Catalyzes the deimination of arginine residues of proteins.<ref>PMID:27866708</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Ca(2+)-dependent enzyme peptidyl-arginine deiminase type III (PAD3) catalyses the deimination of arginine residues to form citrulline residues in proteins such as keratin, filaggrin and trichohyalin. This is an important post-translation modification that is required for normal hair and skin formation in follicles and keratocytes. The structure of apo human PAD3 was determined by X-ray crystallography to a resolution of 2.8 A. The structure of PAD3 revealed a similar overall architecture to other PAD isoforms: the N-terminal and middle domains of PAD3 show sequence and structural variety, whereas the sequence and structure of the C-terminal catalytic domain is highly conserved. Structural analysis indicates that PAD3 is a dimer in solution, as is also the case for the PAD2 and PAD4 isoforms but not the PAD1 isoform.
 
Structural characterization of human peptidyl-arginine deiminase type III by X-ray crystallography.,Rechiche O, Lee TV, Lott JS Acta Crystallogr F Struct Biol Commun. 2021 Oct 1;77(Pt 10):334-340. doi: , 10.1107/S2053230X21009195. Epub 2021 Sep 21. PMID:34605437<ref>PMID:34605437</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ce1" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Protein-arginine deiminase]]
[[Category: Lee TV]]
[[Category: Lee, T V]]
[[Category: Lott JS]]
[[Category: Lott, J S]]
[[Category: Rechiche O]]
[[Category: Rechiche, O]]
[[Category: Citrullination calcium follicle hair skin]]
[[Category: Hydrolase]]
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