Cloned (Comment) | Organism |
---|---|
MetRS DNA and amino acid sequence analysis, phylogenetic tree | Clostridioides difficile |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | MetRS drug design and homology modelling, overview | Clostridioides difficile | |
REP3123 | a selective and potent competitive, versus methionine not ATP, MetRS inhibitor, that strongly binds at the active site, docking study | Clostridioides difficile |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Clostridioides difficile | |
Zn2+ | zinc is an absolute requirement for enzyme activity, binding site residues, overview | Clostridioides difficile |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-methionine + tRNAMet | Clostridioides difficile | - |
AMP + diphosphate + L-methionyl-tRNAMet | - |
? | |
ATP + L-methionine + tRNAMet | Clostridioides difficile 630 | - |
AMP + diphosphate + L-methionyl-tRNAMet | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridioides difficile | Q181D9 | - |
- |
Clostridioides difficile 630 | Q181D9 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-methionine + tRNAMet | - |
Clostridioides difficile | AMP + diphosphate + L-methionyl-tRNAMet | - |
? | |
ATP + L-methionine + tRNAMet | active site analysis and docking study, overview. Key residues are His53, Asp51 and Lys56 consistently forming H-bonding interactions with the carboxylic acid moiety of methionine. Ile12 forms a hydrogen bond with this moiety in different dockings and the residues Ile224, Val226 and Ala230 form a hydrophobic pocket | Clostridioides difficile | AMP + diphosphate + L-methionyl-tRNAMet | - |
? | |
ATP + L-methionine + tRNAMet | - |
Clostridioides difficile 630 | AMP + diphosphate + L-methionyl-tRNAMet | - |
? | |
ATP + L-methionine + tRNAMet | active site analysis and docking study, overview. Key residues are His53, Asp51 and Lys56 consistently forming H-bonding interactions with the carboxylic acid moiety of methionine. Ile12 forms a hydrogen bond with this moiety in different dockings and the residues Ile224, Val226 and Ala230 form a hydrophobic pocket | Clostridioides difficile 630 | AMP + diphosphate + L-methionyl-tRNAMet | - |
? | |
additional information | Met-tRNA anticodon interactions with the MetRS homology model, overview | Clostridioides difficile | ? | - |
? | |
additional information | Met-tRNA anticodon interactions with the MetRS homology model, overview | Clostridioides difficile 630 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | secondary structure and three-dimensional structure molecular modeling, model validation, overview | Clostridioides difficile |
Synonyms | Comment | Organism |
---|---|---|
Methionyl tRNA synthetase | - |
Clostridioides difficile |
MetRS | - |
Clostridioides difficile |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Clostridioides difficile |