Literature summary for 4.6.1.2 extracted from

Agullo, L.; Buch, I.; Gutierrez-de-Teran, H.; Garcia-Dorado, D.; Villa-Freixa, J.
Computational exploration of the binding mode of heme-dependent stimulators into the active catalytic domain of soluble guanylate cyclase (2016), Proteins, 84, 1534-1548 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
homology modeling of the catalytic domain in inactive or active conformations based on PDB entries 2WZ1, 3ET6, 1CJU and molecular dynamics simulations reveals presence of potential high-affinity binding site on the active structure. The site is located between the pseudo-symmetric and the catalytic site just over the loop beta2-beta3 and does not overlap with the forskolin binding site on adenylate cyclases	Homo sapiens

Crystallization (Comment)

Organism

homology modeling of the catalytic domain in inactive or active conformations based on PDB entries 2WZ1, 3ET6, 1CJU and molecular dynamics simulations reveals presence of potential high-affinity binding site on the active structure. The site is located between the pseudo-symmetric and the catalytic site just over the loop beta2-beta3 and does not overlap with the forskolin binding site on adenylate cyclases

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q02153	isoform GUCI1B1	-

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Release 2023.1 (January 2023)