3ET6
The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase
Summary for 3ET6
| Entry DOI | 10.2210/pdb3et6/pdb |
| Descriptor | Soluble guanylyl cyclase beta, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | guanylate cyclase, guanylyl cyclase, dimethylarsenic, lyase, membrane, transmembrane |
| Biological source | Chlamydomonas reinhardtii More |
| Total number of polymer chains | 2 |
| Total formula weight | 43473.80 |
| Authors | Winger, J.A.,Derbyshire, E.R.,Lamers, M.H.,Marletta, M.A.,Kuriyan, J. (deposition date: 2008-10-07, release date: 2008-10-14, Last modification date: 2024-11-20) |
| Primary citation | Winger, J.A.,Derbyshire, E.R.,Lamers, M.H.,Marletta, M.A.,Kuriyan, J. The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase. Bmc Struct.Biol., 8:42-42, 2008 Cited by PubMed Abstract: Soluble guanylate cyclases generate cyclic GMP when bound to nitric oxide, thereby linking nitric oxide levels to the control of processes such as vascular homeostasis and neurotransmission. The guanylate cyclase catalytic module, for which no structure has been determined at present, is a class III nucleotide cyclase domain that is also found in mammalian membrane-bound guanylate and adenylate cyclases. PubMed: 18842118DOI: 10.1186/1472-6807-8-42 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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