Entry Database : PDB / ID : 2cj9 Structure visualization Downloads & linksTitle Crystal structure of Methanosarcina barkeri seryl-tRNA synthetase complexed with an analog of seryladenylate ComponentsSERYL-TRNA SYNTHETASE Details Keywords LIGASE / ZINC ION / SERYLADENYLATE / TRNA SYNTHETASEFunction / homology Function and homology informationFunction Domain/homology Component
selenocysteine biosynthetic process / seryl-tRNA aminoacylation / serine-tRNA ligase / serine-tRNA ligase activity / zinc ion binding / ATP binding / cytoplasm Similarity search - Function Alpha-Beta Plaits - #1920 / Serine-tRNA ligase type 2, archaea / Serine-tRNA ligase type 2, tRNA-binding domain / tRNA-binding domain / Bira Bifunctional Protein; Domain 2 / BirA Bifunctional Protein; domain 2 / Aminoacyl-tRNA synthetase, class II / Aminoacyl-transfer RNA synthetases class-II family profile. / Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) / Alpha-Beta Plaits ... Alpha-Beta Plaits - #1920 / Serine-tRNA ligase type 2, archaea / Serine-tRNA ligase type 2, tRNA-binding domain / tRNA-binding domain / Bira Bifunctional Protein; Domain 2 / BirA Bifunctional Protein; domain 2 / Aminoacyl-tRNA synthetase, class II / Aminoacyl-transfer RNA synthetases class-II family profile. / Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species METHANOSARCINA BARKERI (archaea)Method X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution : 2.3 Å DetailsAuthors Bilokapic, S. / Maier, T. / Ahel, D. / Gruic-Sovulj, I. / Soll, D. / Weygand-Durasevic, I. / Ban, N. CitationJournal : Embo J. / Year : 2006Title : Structure of the Unusual Seryl-tRNA Synthetase Reveals a Distinct Zinc-Dependent Mode of Substrate RecognitionAuthors : Bilokapic, S. / Maier, T. / Ahel, D. / Gruic-Sovulj, I. / Soll, D. / Weygand-Durasevic, I. / Ban, N. History Deposition Mar 29, 2006 Deposition site : PDBE / Processing site : PDBERevision 1.0 Jun 26, 2006 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Advisory / Version format complianceRevision 1.2 May 8, 2019 Group : Data collection / Experimental preparation / OtherCategory : database_PDB_rev / database_PDB_rev_record ... database_PDB_rev / database_PDB_rev_record / exptl_crystal_grow / pdbx_database_proc / pdbx_database_status Item : _exptl_crystal_grow.method / _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approvalRevision 1.3 May 8, 2024 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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.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_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
Show all Show less Remark 650 HELIX DETERMINATION METHOD: AUTHOR PROVIDED. Remark 700 SHEET DETERMINATION METHOD: AUTHOR PROVIDED.