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 Cited by PubMed: 24669844DOI: 10.1021/bi500129k PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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