Entry | Database: PDB / ID: 3swf |
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Title | CNGA1 621-690 containing CLZ domain |
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Components | cGMP-gated cation channel alpha-1 |
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Keywords | TRANSPORT PROTEIN / Coiled-coil / Assembly domain |
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Function / homology | Function and homology information
intracellular cyclic nucleotide activated cation channel complex / intracellularly cGMP-activated cation channel activity / Inactivation, recovery and regulation of the phototransduction cascade / intracellularly cAMP-activated cation channel activity / Activation of the phototransduction cascade / response to stimulus / sodium ion transport / monoatomic cation transmembrane transport / monoatomic cation transport / photoreceptor outer segment ...intracellular cyclic nucleotide activated cation channel complex / intracellularly cGMP-activated cation channel activity / Inactivation, recovery and regulation of the phototransduction cascade / intracellularly cAMP-activated cation channel activity / Activation of the phototransduction cascade / response to stimulus / sodium ion transport / monoatomic cation transmembrane transport / monoatomic cation transport / photoreceptor outer segment / cGMP binding / transmembrane transporter complex / visual perception / calcium ion transport / protein-containing complex binding / plasma membraneSimilarity search - Function Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #300 / Cyclic nucleotide-gated channel, C-terminal leucine zipper domain / C-terminal leucine zipper domain of cyclic nucleotide-gated channels / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Cyclic nucleotide-binding domain signature 2. / Cyclic nucleotide-binding domain signature 1. / Cyclic nucleotide-binding, conserved site / Cyclic nucleotide-monophosphate binding domain / Cyclic nucleotide-binding domain / cAMP/cGMP binding motif profile. ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #300 / Cyclic nucleotide-gated channel, C-terminal leucine zipper domain / C-terminal leucine zipper domain of cyclic nucleotide-gated channels / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Cyclic nucleotide-binding domain signature 2. / Cyclic nucleotide-binding domain signature 1. / Cyclic nucleotide-binding, conserved site / Cyclic nucleotide-monophosphate binding domain / Cyclic nucleotide-binding domain / cAMP/cGMP binding motif profile. / Cyclic nucleotide-binding domain / Cyclic nucleotide-binding domain superfamily / RmlC-like jelly roll fold / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Ion transport domain / Ion transport protein / Up-down Bundle / Mainly AlphaSimilarity search - Domain/homology |
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Biological species | ![](img/tx_mammal.gif) Bos taurus (cattle) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.14 Å |
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Authors | Shuart, N.G. / Haitin, Y. / Camp, S.S. / Black, K.D. / Zagotta, W.N. |
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Citation | Journal: Nat Commun / Year: 2011 Title: Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic nucleotide-gated ion channels. Authors: Shuart, N.G. / Haitin, Y. / Camp, S.S. / Black, K.D. / Zagotta, W.N. |
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History | Deposition | Jul 13, 2011 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Sep 14, 2011 | Provider: repository / Type: Initial release |
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Revision 1.1 | Sep 13, 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 / pdbx_struct_conn_angle / struct_conn / 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 / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _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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