3KT3
Crystal structure of S. cerevisiae tryptophanyl-tRNA synthetase in complex with TrpAMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004830 | molecular_function | tryptophan-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 | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
| A | 1990825 | molecular_function | sequence-specific mRNA binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004830 | molecular_function | tryptophan-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 | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
| B | 1990825 | molecular_function | sequence-specific mRNA binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0004830 | molecular_function | tryptophan-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 | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
| C | 1990825 | molecular_function | sequence-specific mRNA binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| D | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006412 | biological_process | translation |
| D | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| D | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
| D | 1990825 | molecular_function | sequence-specific mRNA binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TYM A 500 |
| Chain | Residue |
| A | TYR106 |
| A | GLU146 |
| A | LYS147 |
| A | GLN230 |
| A | CYS255 |
| A | ALA256 |
| A | ASP258 |
| A | GLN259 |
| A | PHE263 |
| A | ARG284 |
| A | PHE285 |
| A | GLY108 |
| A | PHE286 |
| A | LYS295 |
| A | MET296 |
| A | SO4439 |
| A | HOH464 |
| A | HOH490 |
| A | ARG109 |
| A | GLY110 |
| A | GLY119 |
| A | HIS120 |
| A | PRO123 |
| A | GLU141 |
| A | THR143 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 439 |
| Chain | Residue |
| A | ARG109 |
| A | HIS117 |
| A | HIS120 |
| A | SER297 |
| A | ALA298 |
| A | TYM500 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 440 |
| Chain | Residue |
| A | ALA42 |
| A | GLN43 |
| A | ASN44 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 441 |
| Chain | Residue |
| A | ARG73 |
| A | GLU74 |
| A | HOH504 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 442 |
| Chain | Residue |
| A | PHE148 |
| A | THR155 |
| A | ILE156 |
| A | HOH448 |
| B | ARG199 |
| B | ARG202 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TYM B 700 |
| Chain | Residue |
| B | TYR106 |
| B | THR107 |
| B | GLY108 |
| B | ARG109 |
| B | GLY110 |
| B | GLY119 |
| B | HIS120 |
| B | PRO123 |
| B | GLU141 |
| B | THR143 |
| B | GLU146 |
| B | LYS147 |
| B | GLN230 |
| B | CYS255 |
| B | ALA256 |
| B | ASP258 |
| B | GLN259 |
| B | PHE263 |
| B | PHE286 |
| B | LYS295 |
| B | MET296 |
| B | SO4439 |
| B | HOH461 |
| B | HOH466 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 439 |
| Chain | Residue |
| B | ARG109 |
| B | HIS117 |
| B | HIS120 |
| B | LYS295 |
| B | MET296 |
| B | SER297 |
| B | ALA298 |
| B | TYM700 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 440 |
| Chain | Residue |
| A | ARG199 |
| B | PHE148 |
| B | THR155 |
| B | ILE156 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 441 |
| Chain | Residue |
| B | ARG73 |
| B | GLU74 |
| site_id | BC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TYM C 600 |
| Chain | Residue |
| C | PHE285 |
| C | PHE286 |
| C | LYS295 |
| C | MET296 |
| C | SO4441 |
| C | HOH446 |
| C | HOH463 |
| C | TYR106 |
| C | THR107 |
| C | GLY108 |
| C | ARG109 |
| C | GLY110 |
| C | GLY119 |
| C | HIS120 |
| C | PRO123 |
| C | GLU141 |
| C | THR143 |
| C | GLU146 |
| C | LYS147 |
| C | GLN230 |
| C | CYS255 |
| C | ALA256 |
| C | ASP258 |
| C | GLN259 |
| C | PHE263 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 439 |
| Chain | Residue |
| C | ARG73 |
| C | GLU74 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 440 |
| Chain | Residue |
| C | THR155 |
| C | ILE156 |
| D | ARG199 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 C 441 |
| Chain | Residue |
| C | ARG109 |
| C | HIS117 |
| C | HIS120 |
| C | LYS295 |
| C | MET296 |
| C | SER297 |
| C | ALA298 |
| C | TYM600 |
| site_id | BC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TYM D 800 |
| Chain | Residue |
| D | TYR106 |
| D | THR107 |
| D | GLY108 |
| D | ARG109 |
| D | GLY110 |
| D | GLY119 |
| D | HIS120 |
| D | PRO123 |
| D | GLU141 |
| D | THR143 |
| D | GLU146 |
| D | LYS147 |
| D | GLN230 |
| D | CYS255 |
| D | ALA256 |
| D | ASP258 |
| D | GLN259 |
| D | PHE263 |
| D | ARG284 |
| D | PHE285 |
| D | PHE286 |
| D | LYS295 |
| D | MET296 |
| D | SO4439 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 439 |
| Chain | Residue |
| D | ARG109 |
| D | HIS117 |
| D | HIS120 |
| D | SER297 |
| D | ALA298 |
| D | TYM800 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 D 440 |
| Chain | Residue |
| D | ARG73 |
| D | GLU74 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 441 |
| Chain | Residue |
| C | ARG199 |
| D | PHE148 |
| D | THR155 |
| D | ILE156 |
| D | HOH454 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 11 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Ps.SDsMHLGHM |
| Chain | Residue | Details |
| A | PRO111-MET121 |
