8H99
Crystal structure of E. coli ThrS catalytic domain mutant
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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004829 | molecular_function | threonine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006435 | biological_process | threonyl-tRNA aminoacylation |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11953757 |
| Chain | Residue | Details |
| A | LYS246 | |
| A | ASN342 | |
| A | LEU489 | |
| A | ASP615 | |
| B | LYS246 | |
| B | ASN342 | |
| B | LEU489 | |
| B | ASP615 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10319817, ECO:0007744|PDB:1QF6 |
| Chain | Residue | Details |
| A | HIS309 | |
| B | SER517 | |
| A | VAL376 | |
| A | GLN381 | |
| A | GLN479 | |
| A | SER517 | |
| B | HIS309 | |
| B | VAL376 | |
| B | GLN381 | |
| B | GLN479 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10319817 |
| Chain | Residue | Details |
| A | TYR313 | |
| A | ILE547 | |
| A | ASN575 | |
| A | ARG589 | |
| A | VAL595 | |
| A | ARG609 | |
| B | TYR313 | |
| B | ARG325 | |
| B | TYR348 | |
| B | ARG363 | |
| B | ARG375 | |
| A | ARG325 | |
| B | PHE379 | |
| B | PHE462 | |
| B | GLN484 | |
| B | ARG520 | |
| B | ILE547 | |
| B | ASN575 | |
| B | ARG589 | |
| B | VAL595 | |
| B | ARG609 | |
| A | TYR348 | |
| A | ARG363 | |
| A | ARG375 | |
| A | PHE379 | |
| A | PHE462 | |
| A | GLN484 | |
| A | ARG520 |
| site_id | SWS_FT_FI4 |
| 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 |
| A | CYS334 | |
| A | HIS385 | |
| B | CYS334 | |
| B | HIS385 |
| site_id | SWS_FT_FI5 |
| 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 |
| A | HIS511 | |
| B | HIS511 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS286 | |
| B | LYS286 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 540 |
| Chain | Residue | Details |
| A | CYS334 | electrostatic stabiliser, metal ligand |
| A | ARG363 | electrostatic stabiliser |
| A | GLN381 | electrostatic stabiliser |
| A | ASP383 | electrostatic stabiliser |
| A | HIS385 | metal ligand |
| A | LYS465 | electrostatic stabiliser |
| A | HIS511 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 540 |
| Chain | Residue | Details |
| B | CYS334 | electrostatic stabiliser, metal ligand |
| B | ARG363 | electrostatic stabiliser |
| B | GLN381 | electrostatic stabiliser |
| B | ASP383 | electrostatic stabiliser |
| B | HIS385 | metal ligand |
| B | LYS465 | electrostatic stabiliser |
| B | HIS511 | metal ligand |
