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Literature summary extracted from

  • Li, M.; Wen, F.; Zhao, S.; Wang, P.; Li, S.; Zhang, Y.; Zheng, N.; Wang, J.
    Exploring the molecular basis for binding of inhibitors by threonyl-tRNA synthetase from Brucella abortus A virtual screening study (2016), Int. J. Mol. Sci., 17, E1078 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
6.1.1.3 drug development targeting threonyl-tRNA synthetase (ThrRS) of Brucella abortus is a promising approach to developing small-molecule drugs against bovine brucellosis Brucella abortus

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.1.3 borrelidin predicted binding mode of borrelidin, BaThrRS enzyme homology structure model docking of the ligand, overview Brucella abortus
6.1.1.3 additional information the BaThrRS-binding site structure for inhibitors is analyzed. Virtual database screening for inhibitors of the enzyme using docking studies, free energy of binding between BaThrRS and inhibitors, overview Brucella abortus
6.1.1.3 ZINC27215482 docking analysis, overview. The best inhibitor, which can be used to develop novel drugs against bovine brucellosis Brucella abortus
6.1.1.3 ZINC35270978
-
 Brucella abortus
6.1.1.3 ZINC35458951
-
 Brucella abortus
6.1.1.3 ZINC67910544
-
 Brucella abortus
6.1.1.3 ZINC72320615
-
 Brucella abortus
6.1.1.3 ZINC72320626
-
 Brucella abortus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.3 Mg2+ required Brucella abortus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.3 ATP + L-threonine + tRNAThr Brucella abortus
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.3 Brucella abortus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Brucella abortus AMP + diphosphate + L-threonyl-tRNAThr
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.3 ? x * 74472, sequence calculation Brucella abortus

Synonyms

EC Number Synonyms Comment Organism
6.1.1.3 BaThrRS
-
 Brucella abortus
6.1.1.3 Threonyl-tRNA synthetase
-
 Brucella abortus
6.1.1.3 ThrRS
-
 Brucella abortus
6.1.1.3 ThrS
-
 Brucella abortus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.3 ATP identification of the ATP-binding regions of BaThrRS, docking of ATP to the protein, and modeling of the binding structure, predicted binding mode of ATP, overview Brucella abortus

General Information

EC Number General Information Comment Organism
6.1.1.3 evolution sequence comparison of threonyl-tRNA synthetases from Brucella abortus (BaThrRS) and Escherichia coli (EThrRS), which reveals 51% sequence identity Brucella abortus
6.1.1.3 additional information BaThrRS enzyme structure homology modeling based on the EThrRS structure from Escherichia coli, PDB ID 1QF6, optimization using molecular dynamics simulations, overview. The substrate-binding region in BaThrRS consists of Arg372, Glu374, Phe388, Gln493, Ser531, and Arg534, which correspond to residues Arg363, Glu365, Phe379, Gln479, Ser517, and Arg520 in EThrRS Brucella abortus