5K0S
Crystal structure of methionyl-tRNA synthetase MetRS from Brucella melitensis in complex with inhibitor Chem 1312
Replaces: 4LNEFunctional 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 |
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 |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
C | 0004825 | molecular_function | methionine-tRNA ligase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006412 | biological_process | translation |
C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
C | 0006431 | biological_process | methionyl-tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue 0OU A 601 |
Chain | Residue |
A | ILE12 |
A | ALA233 |
A | TYR237 |
A | HIS269 |
A | TYR14 |
A | ASP51 |
A | HIS53 |
A | GLY54 |
A | MET227 |
A | TYR228 |
A | VAL229 |
A | ASP232 |
site_id | AC2 |
Number of Residues | 16 |
Details | binding site for residue 0OU B 601 |
Chain | Residue |
B | ALA11 |
B | ILE12 |
B | TYR14 |
B | ASP51 |
B | HIS53 |
B | GLY54 |
B | MET227 |
B | TYR228 |
B | VAL229 |
B | ASP232 |
B | ALA233 |
B | TYR237 |
B | HIS269 |
B | HOH726 |
B | HOH727 |
B | HOH757 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue 0OU C 601 |
Chain | Residue |
C | ILE12 |
C | TYR14 |
C | ASP51 |
C | HIS53 |
C | GLY54 |
C | MET227 |
C | TYR228 |
C | VAL229 |
C | ASP232 |
C | ALA233 |
C | TYR237 |
C | HIS269 |
Functional Information from PROSITE/UniProt
site_id | PS00178 |
Number of Residues | 10 |
Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..NGkPHIGHA |
Chain | Residue | Details |
A | PRO15-ALA24 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01228 |
Chain | Residue | Details |
A | LYS303 | |
B | LYS303 | |
C | LYS303 |