4ni2: Difference between revisions
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==Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase== | ==Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase== | ||
<StructureSection load='4ni2' size='340' side='right' caption='[[4ni2]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4ni2' size='340' side='right'caption='[[4ni2]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ni2]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ni2]] is a 2 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=4NI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NI2 FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | |||
<tr><td class="sblockLbl"><b> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ni2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ni2 OCA], [https://pdbe.org/4ni2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ni2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ni2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ni2 ProSAT]</span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </table> | ||
<table> | == Disease == | ||
[https://www.uniprot.org/uniprot/GCYA1_HUMAN GCYA1_HUMAN] Moyamoya disease with early-onset achalasia. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GCYA1_HUMAN GCYA1_HUMAN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Interfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: heterodimerization is required but not sufficient for activity.,Seeger F, Quintyn R, Tanimoto A, Williams GJ, Tainer JA, Wysocki VH, Garcin ED Biochemistry. 2014 Apr 8;53(13):2153-65. doi: 10.1021/bi500129k. Epub 2014 Mar, 26. PMID:24669844<ref>PMID:24669844</ref> | Interfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: heterodimerization is required but not sufficient for activity.,Seeger F, Quintyn R, Tanimoto A, Williams GJ, Tainer JA, Wysocki VH, Garcin ED Biochemistry. 2014 Apr 8;53(13):2153-65. doi: 10.1021/bi500129k. Epub 2014 Mar, 26. PMID:24669844<ref>PMID:24669844</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ni2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Guanylate cyclase 3D structures|Guanylate cyclase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Garcin | [[Category: Garcin ED]] | ||
[[Category: Seeger | [[Category: Seeger F]] | ||
[[Category: Tainer | [[Category: Tainer JA]] | ||
[[Category: Williams | [[Category: Williams GJ]] | ||