View source for 8hbh


==Structure of human soluble guanylate cyclase in the NO-activated state at 3.1 angstrom==
<StructureSection load='8hbh' size='340' side='right'caption='[[8hbh]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hbh]] 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=8HBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HBH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene></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=8hbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hbh OCA], [https://pdbe.org/8hbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hbh RCSB], [https://www.ebi.ac.uk/pdbsum/8hbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hbh ProSAT]</span></td></tr>
</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;">
== Publication Abstract from PubMed ==
Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO). The binding of NO to the haem of sGC induces a large conformational change in the enzyme and activates its cyclase activity. However, whether NO binds to the proximal site or the distal site of haem in the fully activated state remains under debate. Here, we present cryo-EM maps of sGC in the NO-activated state at high resolutions, allowing the observation of the density of NO. These cryo-EM maps show the binding of NO to the distal site of haem in the NO-activated state.

NO binds to the distal site of haem in the fully activated soluble guanylate cyclase.,Liu R, Kang Y, Chen L Nitric Oxide. 2023 May 1;134-135:17-22. doi: 10.1016/j.niox.2023.03.002. Epub , 2023 Mar 25. PMID:36972843<ref>PMID:36972843</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8hbh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Guanylate cyclase 3D structures|Guanylate cyclase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chen L]]
[[Category: Liu R]]