4PY2
Crystal structure of methionyl-tRNA synthetase MetRS from Brucella melitensis in complex with inhibitor 1-{3-[(3,5-DICHLOROBENZYL)AMINO]PROPYL}-3-THIOPHEN-3-YLUREA
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 |
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 43E A 601 |
Chain | Residue |
A | ILE12 |
A | TYR237 |
A | ILE265 |
A | HOH826 |
A | TYR14 |
A | ASP51 |
A | HIS53 |
A | GLY54 |
A | MET227 |
A | VAL229 |
A | TRP230 |
A | ASP232 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 602 |
Chain | Residue |
A | ARG35 |
A | ARG38 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE 43E 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 | TYR237 |
B | ILE265 |
B | HIS269 |
B | HOH706 |
B | HOH776 |
B | HOH922 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 602 |
Chain | Residue |
B | ARG35 |
B | ARG38 |
B | HOH936 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 603 |
Chain | Residue |
B | PRO68 |
B | ARG69 |
B | TRP215 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 604 |
Chain | Residue |
B | LEU320 |
B | ASP321 |
B | GLN322 |
B | GLN466 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 605 |
Chain | Residue |
B | ARG80 |
B | GLU84 |
B | ASN90 |
B | HOH795 |
B | HOH903 |
site_id | AC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 43E C 601 |
Chain | Residue |
C | ILE12 |
C | TYR14 |
C | ASP51 |
C | HIS53 |
C | GLY54 |
C | MET227 |
C | TYR228 |
C | VAL229 |
C | TRP230 |
C | ASP232 |
C | TYR237 |
C | HIS269 |
C | HOH733 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 602 |
Chain | Residue |
C | THR67 |
C | PRO68 |
C | ARG69 |
C | HOH743 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 603 |
Chain | Residue |
C | TYR119 |
C | GLY121 |
C | GLY122 |
C | PHE165 |
C | HOH752 |
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 |