2CSX
Crystal structure of Aquifex aeolicus methionyl-tRNA synthetase complexed with tRNA(Met)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004825 | molecular_function | methionine-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006412 | biological_process | translation |
A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
A | 0006431 | biological_process | methionyl-tRNA aminoacylation |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004825 | molecular_function | methionine-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006412 | biological_process | translation |
B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
B | 0006431 | biological_process | methionyl-tRNA aminoacylation |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | CYS129 | |
B | LYS298 | |
A | CYS132 | |
A | CYS147 | |
A | HIS150 | |
A | LYS298 | |
B | CYS129 | |
B | CYS132 | |
B | CYS147 | |
B | HIS150 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a8h |
Chain | Residue | Details |
A | LYS298 | |
A | LYS295 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a8h |
Chain | Residue | Details |
B | LYS298 | |
B | LYS295 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a8h |
Chain | Residue | Details |
A | LYS298 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a8h |
Chain | Residue | Details |
B | LYS298 |