8OU8
Crystal structure of E. coli threonyl tRNA synthetase in complex with a TM84 analogue
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004829 | molecular_function | threonine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006435 | biological_process | threonyl-tRNA aminoacylation |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| D | 0004829 | molecular_function | threonine-tRNA ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| D | 0006435 | biological_process | threonyl-tRNA aminoacylation |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:10319817, ECO:0000269|PubMed:10881191, ECO:0000269|PubMed:11136973, ECO:0000269|PubMed:11953757 |
| Chain | Residue | Details |
| D | CYS93 | |
| D | HIS144 | |
| A | CYS93 | |
| A | HIS144 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:10319817, ECO:0000269|PubMed:10881191, ECO:0000269|PubMed:11136973 |
| Chain | Residue | Details |
| D | HIS270 | |
| A | HIS270 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| D | LYS45 | |
| A | LYS45 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11953757 |
| Chain | Residue | Details |
| D | LYS5 | |
| D | ASN101 | |
| D | LEU248 | |
| D | ASP374 | |
| A | LYS5 | |
| A | ASN101 | |
| A | LEU248 | |
| A | ASP374 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10319817, ECO:0007744|PDB:1QF6 |
| Chain | Residue | Details |
| D | HIS68 | |
| A | SER276 | |
| D | VAL135 | |
| D | GLN140 | |
| D | GLN238 | |
| D | SER276 | |
| A | HIS68 | |
| A | VAL135 | |
| A | GLN140 | |
| A | GLN238 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10319817 |
| Chain | Residue | Details |
| D | TYR72 | |
| D | ILE306 | |
| D | ASN334 | |
| D | ARG348 | |
| D | VAL354 | |
| D | ARG368 | |
| A | TYR72 | |
| A | ARG84 | |
| A | TYR107 | |
| A | ARG122 | |
| A | ARG134 | |
| D | ARG84 | |
| A | PHE138 | |
| A | TYR221 | |
| A | GLN243 | |
| A | ARG279 | |
| A | ILE306 | |
| A | ASN334 | |
| A | ARG348 | |
| A | VAL354 | |
| A | ARG368 | |
| D | TYR107 | |
| D | ARG122 | |
| D | ARG134 | |
| D | PHE138 | |
| D | TYR221 | |
| D | GLN243 | |
| D | ARG279 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 540 |
| Chain | Residue | Details |
| D | CYS93 | electrostatic stabiliser, metal ligand |
| D | ARG122 | electrostatic stabiliser |
| D | GLN140 | electrostatic stabiliser |
| D | ASP142 | electrostatic stabiliser |
| D | HIS144 | metal ligand |
| D | LYS224 | electrostatic stabiliser |
| D | HIS270 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 540 |
| Chain | Residue | Details |
| A | CYS93 | electrostatic stabiliser, metal ligand |
| A | ARG122 | electrostatic stabiliser |
| A | GLN140 | electrostatic stabiliser |
| A | ASP142 | electrostatic stabiliser |
| A | HIS144 | metal ligand |
| A | LYS224 | electrostatic stabiliser |
| A | HIS270 | metal ligand |
