Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	NO binds to the distal site of haem in the fully activated soluble guanylate cyclase.
Journal, issue, pages	Nitric Oxide, Vol. 134-135, Page 17-22, Year 2023
Publish date	May 1, 2023
Authors	Rui Liu / Yunlu Kang / Lei Chen /
PubMed Abstract	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 ...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.
External links	Nitric Oxide / PubMed:36972843
Methods	EM (single particle)
Resolution	3.1 - 3.2 Å
Structure data	34623 8hbe EMDB-34623, PDB-8hbe: Structure of human soluble guanylate cyclase in the inactive state at 3.1 angstrom Method: EM (single particle) / Resolution: 3.2 Å EMDB-34624: Consensus map of human soluble guanylate cyclase in the inactive state at 3.2 angstrom Method: EM (single particle) / Resolution: 3.2 Å EMDB-34625: Focus refined map of N-lobe of soluble guanylate cyclase in the inactive state at 3.1 angstrom Method: EM (single particle) / Resolution: 3.1 Å EMDB-34626: Focus refined map of C-lobe of human soluble guanylate cyclase in the inactive state at 3.1 angstrom Method: EM (single particle) / Resolution: 3.1 Å 34627 8hbf EMDB-34627, PDB-8hbf: Structure of human soluble guanylate cyclase in the NO+Rio state at 3.1 angstrom Method: EM (single particle) / Resolution: 3.1 Å EMDB-34628: Consensus map of human soluble guanylate cyclase in complex with riociguat in the presence of NO at 3.1 angstrom Method: EM (single particle) / Resolution: 3.1 Å EMDB-34629: Focus refined map of N-lobe of human soluble guanylate cyclase in the NO+Rio state at 3.1 angstrom Method: EM (single particle) / Resolution: 3.1 Å EMDB-34631: Focus refined map of C-lobe of human soluble guanylate cyclase in the NO+Rio state at 3.1 angstrom Method: EM (single particle) / Resolution: 3.1 Å 34632 8hbh EMDB-34632, PDB-8hbh: Structure of human soluble guanylate cyclase in the NO-activated state at 3.1 angstrom Method: EM (single particle) / Resolution: 3.1 Å EMDB-34633: Consensus map of huamn soluble guanylate cyclase in the NO-activated state at 3.2 angstrom Method: EM (single particle) / Resolution: 3.2 Å EMDB-34634: Focus refined map of N-lobe of human soluble guanylate cyclase in the NO-activated state at 3.1 angstrom Method: EM (single particle) / Resolution: 3.1 Å EMDB-34635: Focus refined map of C-lobe of human soluble guanylate cyclase in the NO-activated state at 3.1 angstrom Method: EM (single particle) / Resolution: 3.1 Å
Chemicals	ChemComp-HEM: PROTOPORPHYRIN IX CONTAINING FE ChemComp-G2P: PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-CPP, energy-carrying molecule analogueYM ChemComp-MG: Unknown entry ChemComp-GZO: methyl ~{N}-[4,6-bis(azanyl)-2-[1-[(2-fluorophenyl)methyl]pyrazolo[3,4-b]pyridin-3-yl]pyrimidin-5-yl]-~{N}-methyl-carbamate / medicationYM ChemComp-NO: NITRIC OXIDE
Source	homo sapiens (human)
Keywords	SIGNALING PROTEIN / soluble guanylate cyclase