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 |