Entry | Database: PDB / ID: 2lwr |
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Title | Solution Structure of RING2 Domain from Parkin |
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Components | SD01679p |
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Keywords | LIGASE / Parkin / RING / E3 ligase / Zn-binding / METAL BINDING PROTEIN / STRUCTURAL PROTEIN |
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Function / homology | Function and homology information
positive regulation of compound eye pigmentation / positive regulation of locomotor rhythm / PINK1-PRKN Mediated Mitophagy / Josephin domain DUBs / sperm mitochondrion organization / larval locomotory behavior / Antigen processing: Ubiquitination & Proteasome degradation / Aggrephagy / parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization / positive regulation of neuronal action potential ...positive regulation of compound eye pigmentation / positive regulation of locomotor rhythm / PINK1-PRKN Mediated Mitophagy / Josephin domain DUBs / sperm mitochondrion organization / larval locomotory behavior / Antigen processing: Ubiquitination & Proteasome degradation / Aggrephagy / parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization / positive regulation of neuronal action potential / negative regulation of mitochondrial fusion / RBR-type E3 ubiquitin transferase / positive regulation of autophagy of mitochondrion / positive regulation of mitophagy / regulation of cellular response to oxidative stress / autophagy of mitochondrion / negative regulation of JNK cascade / mitochondrial fission / ubiquitin conjugating enzyme binding / regulation of mitochondrion organization / positive regulation of mitochondrial fission / oogenesis / protein monoubiquitination / protein autoubiquitination / ubiquitin ligase complex / mitochondrion organization / adult locomotory behavior / negative regulation of protein phosphorylation / neuron cellular homeostasis / protein polyubiquitination / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / ubiquitin-dependent protein catabolic process / spermatogenesis / regulation of apoptotic process / response to oxidative stress / protein ubiquitination / Golgi apparatus / endoplasmic reticulum / mitochondrion / zinc ion binding / cytoplasm / cytosolSimilarity search - Function : / : / : / E3 ubiquitin-protein ligase parkin / RING/Ubox-like zinc-binding domain / Parkin, RING/Ubox like zinc-binding domain / RING/Ubox like zinc-binding domain / RING/Ubox like zinc-binding domain / E3 ubiquitin ligase RBR family / IBR domain ...: / : / : / E3 ubiquitin-protein ligase parkin / RING/Ubox-like zinc-binding domain / Parkin, RING/Ubox like zinc-binding domain / RING/Ubox like zinc-binding domain / RING/Ubox like zinc-binding domain / E3 ubiquitin ligase RBR family / IBR domain / In Between Ring fingers / TRIAD supradomain / TRIAD supradomain profile. / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Zinc finger, RING/FYVE/PHD-type / Ubiquitin-like domain superfamilySimilarity search - Domain/homology |
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Biological species | ![](img/tx_arthropod.gif) Drosophila melanogaster (fruit fly) |
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Method | SOLUTION NMR / torsion angle dynamics |
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Model details | closest to the average, model 3 |
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Authors | Mercier, P. / Spratt, D.E. / Manczyk, N. / Shaw, G.S. |
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Citation | Journal: Nat Commun / Year: 2013 Title: A molecular explanation for the recessive nature of parkin-linked Parkinson's disease. Authors: Spratt, D.E. / Julio Martinez-Torres, R. / Noh, Y.J. / Mercier, P. / Manczyk, N. / Barber, K.R. / Aguirre, J.D. / Burchell, L. / Purkiss, A. / Walden, H. / Shaw, G.S. |
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History | Deposition | Aug 6, 2012 | Deposition site: BMRB / Processing site: RCSB |
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Revision 1.0 | Jun 12, 2013 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jul 3, 2013 | Group: Database references |
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Revision 1.2 | Oct 15, 2014 | Group: Structure summary |
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Revision 1.3 | Jun 14, 2023 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / 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_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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_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_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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Revision 1.4 | May 15, 2024 | Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI |
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