Entry | Database: PDB / ID: 4ni2 |
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Title | Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase |
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Components | - Guanylate cyclase soluble subunit alpha-3
- Guanylate cyclase soluble subunit beta-1
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Keywords | LYASE / heterodimeric / cGMP biosynthesis / nitric oxide / cyclase / GTP-binding / metal-binding / nucleotide binding / CYTOSOL |
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Function / homology | Function and homology information
retrograde trans-synaptic signaling by nitric oxide, modulating synaptic transmission / cytidylate cyclase activity / trans-synaptic signaling by nitric oxide, modulating synaptic transmission / guanylate cyclase / guanylate cyclase complex, soluble / cGMP biosynthetic process / guanylate cyclase activity / presynaptic active zone cytoplasmic component / response to oxygen levels / Nitric oxide stimulates guanylate cyclase ...retrograde trans-synaptic signaling by nitric oxide, modulating synaptic transmission / cytidylate cyclase activity / trans-synaptic signaling by nitric oxide, modulating synaptic transmission / guanylate cyclase / guanylate cyclase complex, soluble / cGMP biosynthetic process / guanylate cyclase activity / presynaptic active zone cytoplasmic component / response to oxygen levels / Nitric oxide stimulates guanylate cyclase / relaxation of vascular associated smooth muscle / adenylate cyclase activity / blood circulation / positive regulation of nitric oxide mediated signal transduction / cGMP-mediated signaling / Smooth Muscle Contraction / cellular response to nitric oxide / GABA-ergic synapse / nitric oxide mediated signal transduction / nitric oxide-cGMP-mediated signaling / Hsp90 protein binding / regulation of blood pressure / signaling receptor activity / glutamatergic synapse / heme binding / protein-containing complex binding / GTP binding / metal ion binding / cytosolSimilarity search - Function Haem NO binding associated domain superfamily / Haem NO binding associated / Heme NO binding associated / Nucleotide cyclase, GGDEF domain / Heme NO-binding / H-NOX domain superfamily / Haem-NO-binding / Adenylyl cyclase class-4/guanylyl cyclase, conserved site / Guanylate cyclase signature. / NO signalling/Golgi transport ligand-binding domain superfamily ...Haem NO binding associated domain superfamily / Haem NO binding associated / Heme NO binding associated / Nucleotide cyclase, GGDEF domain / Heme NO-binding / H-NOX domain superfamily / Haem-NO-binding / Adenylyl cyclase class-4/guanylyl cyclase, conserved site / Guanylate cyclase signature. / NO signalling/Golgi transport ligand-binding domain superfamily / Adenylyl- / guanylyl cyclase, catalytic domain / Adenylyl cyclase class-3/4/guanylyl cyclase / Adenylate and Guanylate cyclase catalytic domain / Guanylate cyclase domain profile. / Nucleotide cyclase / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha BetaSimilarity search - Domain/homology |
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Biological species | Homo sapiens (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.9 Å |
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Authors | Seeger, F. / Williams, G.J. / Tainer, J.A. / Garcin, E.D. |
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Citation | Journal: Biochemistry / Year: 2014 Title: Interfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: heterodimerization is required but not sufficient for activity. Authors: Seeger, F. / Quintyn, R. / Tanimoto, A. / Williams, G.J. / Tainer, J.A. / Wysocki, V.H. / Garcin, E.D. |
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History | Deposition | Nov 5, 2013 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Apr 16, 2014 | Provider: repository / Type: Initial release |
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Revision 1.1 | May 7, 2014 | Group: Database references |
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Revision 1.2 | Nov 22, 2017 | Group: Refinement description / Category: software / Item: _software.classification / _software.name |
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Revision 1.3 | Sep 20, 2023 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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