- PDB-1lyl: LYSYL-TRNA SYNTHETASE (LYSU) (E.C.6.1.1.6) COMPLEXED WITH LYSINE -
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Basic information
Entry
Database: PDB / ID: 1lyl
Title
LYSYL-TRNA SYNTHETASE (LYSU) (E.C.6.1.1.6) COMPLEXED WITH LYSINE
Components
LYSYL-TRNA SYNTHETASE (LYSU)
Keywords
LIGASE (SYNTHETASE)
Function / homology
Function and homology information
RNA capping / lysine-tRNA ligase / lysine-tRNA ligase activity / lysyl-tRNA aminoacylation / tRNA aminoacylation for protein translation / ligase activity / cellular response to heat / tRNA binding / magnesium ion binding / protein homodimerization activity ...RNA capping / lysine-tRNA ligase / lysine-tRNA ligase activity / lysyl-tRNA aminoacylation / tRNA aminoacylation for protein translation / ligase activity / cellular response to heat / tRNA binding / magnesium ion binding / protein homodimerization activity / ATP binding / membrane / cytosol Similarity search - Function
Bacterial/eukaryotic lysine-tRNA ligase, class II / Lysine-tRNA ligase, class II, N-terminal / Lysine-tRNA ligase, class II / Lysyl-tRNA synthetase, class II, C-terminal / Aminoacyl-tRNA synthetase, class II (D/K/N) / tRNA synthetases class II (D, K and N) / OB-fold nucleic acid binding domain, AA-tRNA synthetase-type / OB-fold nucleic acid binding domain / Bira Bifunctional Protein; Domain 2 / BirA Bifunctional Protein; domain 2 ...Bacterial/eukaryotic lysine-tRNA ligase, class II / Lysine-tRNA ligase, class II, N-terminal / Lysine-tRNA ligase, class II / Lysyl-tRNA synthetase, class II, C-terminal / Aminoacyl-tRNA synthetase, class II (D/K/N) / tRNA synthetases class II (D, K and N) / OB-fold nucleic acid binding domain, AA-tRNA synthetase-type / OB-fold nucleic acid 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) / Nucleic acid-binding proteins / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Nucleic acid-binding, OB-fold / Beta Barrel / 2-Layer Sandwich / Mainly Beta / Alpha Beta Similarity search - Domain/homology
SYMMETRY THE CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS PRESENTED BELOW GENERATE THE SUBUNITS OF THE POLYMERIC MOLECULE. APPLIED TO RESIDUES: B 14 .. 504 CRYSTALLOGRAPHIC DYAD OPERATION SYMMETRY1 1 1.000000 0.000000 0.000000 0.00000 SYMMETRY2 1 0.000000 -1.000000 0.000000 257.80000 SYMMETRY3 1 0.000000 0.000000 -1.000000 182.08000 APPLIED TO RESIDUES: Y 1 .. 1 CRYSTALLOGRAPHIC DYAD OPERATION SYMMETRY1 2 1.000000 0.000000 0.000000 0.00000 SYMMETRY2 2 0.000000 -1.000000 0.000000 257.80000 SYMMETRY3 2 0.000000 0.000000 -1.000000 182.08000 THE ASYMMETRIC UNIT CAN ALSO BE DESCRIBED AS CONTAINING THREE SUBUNITS ARRANGED AROUND A PSEUDO 31 AXIS PARALLEL TO THE CRYSTALLOGRAPHIC C AXIS, RELATING SUBUNITS *B*, *A* AND *C'* WHERE *C'* IS CRYSTALLOGRAPHICALLY RELATED TO SUBUNIT *C*.
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Components
#1: Protein
LYSYL-TRNASYNTHETASE (LYSU)
Mass: 57767.191 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A8N5, lysine-tRNA ligase
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