4NI2

Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase

Summary for 4NI2

• Entry DOI: 10.2210/pdb4ni2/pdb
• Descriptor: Guanylate cyclase soluble subunit alpha-3, Guanylate cyclase soluble subunit beta-1, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: heterodimeric, lyase, cgmp biosynthesis, nitric oxide, cyclase, gtp-binding, metal-binding, nucleotide binding, cytosol
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : Q02108 Q02153
• Total number of polymer chains: 2
• Total formula weight: 45725.72

Authors

Seeger, F.,Williams, G.J.,Tainer, J.A.,Garcin, E.D. (deposition date: 2013-11-05, release date: 2014-04-16, Last modification date: 2023-09-20)

• Primary citation: Seeger, F.,Quintyn, R.,Tanimoto, A.,Williams, G.J.,Tainer, J.A.,Wysocki, V.H.,Garcin, E.D.; Interfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: heterodimerization is required but not sufficient for activity.; Biochemistry, 53:2153-2165, 2014; PubMed: 24669844; DOI: 10.1021/bi500129k

Experimental method

X-RAY DIFFRACTION (1.9 Å)