5K0T
Crystal structure of methionyl-tRNA synthetase MetRS from Brucella melitensis in complex with inhibitor Chem 1415
Replaces: 4PPWFunctional 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 415 A 601 |
| Chain | Residue |
| A | ILE12 |
| A | TYR237 |
| A | PHE268 |
| A | HIS269 |
| A | TYR14 |
| A | ASP51 |
| A | HIS53 |
| A | GLY54 |
| A | MET227 |
| A | TYR228 |
| A | VAL229 |
| A | TRP230 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 602 |
| Chain | Residue |
| A | LYS18 |
| A | PRO19 |
| A | HIS20 |
| A | ILE309 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 603 |
| Chain | Residue |
| A | ASP70 |
| B | PHE295 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 604 |
| Chain | Residue |
| A | GLU330 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 605 |
| Chain | Residue |
| A | ASP73 |
| A | SER77 |
| A | ARG80 |
| A | ARG95 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | binding site for residue 415 B 601 |
| Chain | Residue |
| B | ILE12 |
| B | TYR14 |
| B | ASP51 |
| B | HIS53 |
| B | GLY54 |
| B | PHE213 |
| B | MET227 |
| B | TYR228 |
| B | VAL229 |
| B | TRP230 |
| B | ASP232 |
| B | ALA233 |
| B | LEU234 |
| B | TYR237 |
| B | ILE265 |
| B | PHE268 |
| B | HIS269 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 602 |
| Chain | Residue |
| B | GLY17 |
| B | HIS20 |
| C | GLU510 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 603 |
| Chain | Residue |
| B | ASP390 |
| B | ASP393 |
| B | ALA394 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 604 |
| Chain | Residue |
| B | ASP404 |
| B | ASP405 |
| site_id | AD1 |
| Number of Residues | 15 |
| Details | binding site for residue 415 C 601 |
| Chain | Residue |
| C | ALA11 |
| C | ILE12 |
| C | TYR14 |
| C | ASP51 |
| C | HIS53 |
| C | GLY54 |
| C | MET227 |
| C | VAL229 |
| C | TRP230 |
| C | ASP232 |
| C | ALA233 |
| C | LEU234 |
| C | TYR237 |
| C | PHE268 |
| C | HIS269 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO C 602 |
| Chain | Residue |
| C | GLU64 |
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 |
