Entry | Database: PDB / ID: 6r4v |
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Title | Crystal structure of human geranylgeranyl diphosphate synthase bound to ibandronate |
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Components | Geranylgeranyl pyrophosphate synthase |
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Keywords | TRANSFERASE / Bisphosphonate / ibandronate / geranylgeranyl diphosphate / prenyltransferase |
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Function / homology | Function and homology information
isoprenoid metabolic process / plastoquinone biosynthetic process / geranylgeranyl diphosphate biosynthetic process / geranylgeranyl diphosphate synthase / transferase complex / Transferases; Transferring alkyl or aryl groups, other than methyl groups / geranyl diphosphate biosynthetic process / dimethylallyltranstransferase / (2E,6E)-farnesyl diphosphate synthase / prenyltransferase activity ...isoprenoid metabolic process / plastoquinone biosynthetic process / geranylgeranyl diphosphate biosynthetic process / geranylgeranyl diphosphate synthase / transferase complex / Transferases; Transferring alkyl or aryl groups, other than methyl groups / geranyl diphosphate biosynthetic process / dimethylallyltranstransferase / (2E,6E)-farnesyl diphosphate synthase / prenyltransferase activity / Cholesterol biosynthesis / farnesyltranstransferase activity / ubiquinone biosynthetic process / isoprenoid biosynthetic process / farnesyl diphosphate biosynthetic process / dimethylallyltranstransferase activity / geranyltranstransferase activity / Activation of gene expression by SREBF (SREBP) / Z disc / perinuclear region of cytoplasm / mitochondrion / nucleoplasm / identical protein binding / metal ion binding / cytoplasm / cytosolSimilarity search - Function Polyprenyl synthases signature 1. / Polyprenyl synthases signature 2. / Polyprenyl synthetase, conserved site / Polyprenyl synthetase / Polyprenyl synthetase / Farnesyl Diphosphate Synthase / Farnesyl Diphosphate Synthase / Isoprenoid synthase domain superfamily / Orthogonal Bundle / Mainly AlphaSimilarity search - Domain/homology |
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Biological species | Homo sapiens (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.202 Å |
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Authors | Lisnyansky, M. / Giladi, M. / Haitin, Y. |
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Funding support | Israel, Germany, 4items Organization | Grant number | Country |
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Israel Science Foundation | 1775/12 and 1721/16 | Israel | German Research Foundation | I-2425-418.13/2016 | Germany | Other private | Shtacher Foundation | Israel | Other private | Israel Cancer Research Foundation Grant 01214 | Israel |
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Citation | Journal: Mol.Pharmacol. / Year: 2019 Title: Metal Coordination Is Crucial for Geranylgeranyl Diphosphate Synthase-Bisphosphonate Interactions: A Crystallographic and Computational Analysis. Authors: Lisnyansky, M. / Yariv, E. / Segal, O. / Marom, M. / Loewenstein, A. / Ben-Tal, N. / Giladi, M. / Haitin, Y. |
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History | Deposition | Mar 24, 2019 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | Sep 18, 2019 | Provider: repository / Type: Initial release |
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Revision 1.1 | Oct 9, 2019 | Group: Data collection / Database references / Category: citation Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title |
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Revision 1.2 | Jan 24, 2024 | 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_conn_type 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_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_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.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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_type.id |
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