1NYR
Structure of Staphylococcus aureus threonyl-tRNA synthetase complexed with ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| 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 | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006435 | biological_process | threonyl-tRNA aminoacylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0043039 | biological_process | tRNA aminoacylation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000049 | molecular_function | tRNA binding |
| 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 | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006435 | biological_process | threonyl-tRNA aminoacylation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0043039 | biological_process | tRNA aminoacylation |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | CYS336 |
| A | HIS387 |
| A | HIS517 |
| A | THR1004 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1002 |
| Chain | Residue |
| A | HIS75 |
| A | HIS79 |
| A | CYS181 |
| A | HIS185 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 2001 |
| Chain | Residue |
| B | HIS387 |
| B | HIS517 |
| B | THR2004 |
| B | CYS336 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP A 1003 |
| Chain | Residue |
| A | ARG365 |
| A | GLU367 |
| A | ARG377 |
| A | VAL378 |
| A | MET381 |
| A | LEU383 |
| A | LYS471 |
| A | THR485 |
| A | LEU486 |
| A | GLN490 |
| A | SER522 |
| A | THR523 |
| A | ARG526 |
| A | THR1004 |
| A | HOH1112 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE THR A 1004 |
| Chain | Residue |
| A | MET334 |
| A | ASN335 |
| A | CYS336 |
| A | ARG365 |
| A | ASP385 |
| A | HIS387 |
| A | GLN490 |
| A | HIS517 |
| A | ZN1001 |
| A | ATP1003 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP B 2003 |
| Chain | Residue |
| B | TYR313 |
| B | MET363 |
| B | ARG365 |
| B | GLU367 |
| B | GLN376 |
| B | ARG377 |
| B | VAL378 |
| B | MET381 |
| B | GLU464 |
| B | THR485 |
| B | SER522 |
| B | THR523 |
| B | ARG526 |
| B | THR2004 |
| B | HOH2068 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE THR B 2004 |
| Chain | Residue |
| B | MET334 |
| B | CYS336 |
| B | ASP385 |
| B | HIS387 |
| B | TYR468 |
| B | GLN490 |
| B | HIS517 |
| B | ZN2001 |
| B | ATP2003 |
| B | HOH2016 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:12875846 |
| Chain | Residue | Details |
| B | HIS387 | |
| B | HIS517 | |
| A | CYS336 | |
| A | HIS387 | |
| A | HIS517 | |
| B | CYS336 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12875846 |
| Chain | Residue | Details |
| A | TYR468 | |
| A | LYS471 | |
| A | THR485 | |
| A | SER522 | |
| B | ARG365 | |
| B | ARG377 | |
| B | TYR468 | |
| B | LYS471 | |
| B | THR485 | |
| B | SER522 | |
| A | ARG365 | |
| A | ARG377 |
