Entry Database : PDB / ID : 2j3l Structure visualization Downloads & linksTitle Prolyl-tRNA synthetase from Enterococcus faecalis complexed with a prolyl-adenylate analogue ('5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE) ComponentsPROLYL-TRNA SYNTHETASE Details Keywords LIGASE / BACTERIAL-TYPE PROLYL-TRNA SYNTHETASE / CLASS II AMINOACYL- TRNA SYNTHETASE / EDITING / TRANSLATION / ATP + L-PROLINE + TRNA (PRO) GIVES AMP + PPI + L-PROLYL-TRNA(PRO)Function / homology Function and homology informationFunction Domain/homology Component
proline-tRNA ligase / proline-tRNA ligase activity / prolyl-tRNA aminoacylation / aminoacyl-tRNA editing activity / transferase activity / ATP binding / cytosol Similarity search - Function Prolyl-tRNA synthetase, class IIa, type 1 / Prolyl-tRNA synthetase, class IIa, bacterial-type / Prokaryote proline-tRNA ligase core domain / Proline--tRNA ligase, anticodon binding domain / YbaK protein / YbaK/aminoacyl-tRNA synthetase-associated domain / YbaK/aminoacyl-tRNA synthetase-associated domain / Aminoacyl-tRNA editing domain / YbaK/aminoacyl-tRNA synthetase-associated domain superfamily / Proline-tRNA ligase, class IIa ... Prolyl-tRNA synthetase, class IIa, type 1 / Prolyl-tRNA synthetase, class IIa, bacterial-type / Prokaryote proline-tRNA ligase core domain / Proline--tRNA ligase, anticodon binding domain / YbaK protein / YbaK/aminoacyl-tRNA synthetase-associated domain / YbaK/aminoacyl-tRNA synthetase-associated domain / Aminoacyl-tRNA editing domain / YbaK/aminoacyl-tRNA synthetase-associated domain superfamily / Proline-tRNA ligase, class IIa / Anticodon-binding domain / Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) / tRNA synthetase class II core domain (G, H, P, S and T) / Anticodon-binding / Anticodon binding domain / Anticodon-binding domain superfamily / 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 Complex / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species ENTEROCOCCUS FAECALIS (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.3 Å DetailsAuthors Crepin, T. / Yaremchuk, A. / Tukalo, M. / Cusack, S. CitationJournal : Structure / Year : 2006Title : Structures of Two Bacterial Prolyl-tRNA Synthetases with and without a Cis-Editing Domain.Authors : Crepin, T. / Yaremchuk, A. / Tukalo, M. / Cusack, S. History Deposition Aug 22, 2006 Deposition site : PDBE / Processing site : PDBERevision 1.0 Oct 11, 2006 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Advisory / Version format complianceRevision 1.2 May 1, 2024 Group : Data collection / Database references ... Data collection / Database references / Other / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Show all Show less Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.