6R1M
Crystal structure of E. coli seryl-tRNA synthetase complexed to seryl sulfamoyl adenosine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004828 | molecular_function | serine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006434 | biological_process | seryl-tRNA aminoacylation |
| A | 0016260 | biological_process | selenocysteine biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004828 | molecular_function | serine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006434 | biological_process | seryl-tRNA aminoacylation |
| B | 0016260 | biological_process | selenocysteine biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue SSA A 501 |
| Chain | Residue |
| A | THR237 |
| A | GLU355 |
| A | ILE356 |
| A | SER357 |
| A | SER358 |
| A | ASN389 |
| A | SER391 |
| A | ALA394 |
| A | ARG397 |
| A | HOH606 |
| A | HOH623 |
| A | GLU239 |
| A | HOH855 |
| A | ARG268 |
| A | GLU270 |
| A | ILE282 |
| A | ARG283 |
| A | MET284 |
| A | PHE287 |
| A | GLU291 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 502 |
| Chain | Residue |
| A | ARG283 |
| A | ARG354 |
| A | GLU355 |
| A | ARG397 |
| A | HOH815 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | MET165 |
| A | HIS173 |
| A | MET284 |
| A | GLN286 |
| A | PHE287 |
| A | ASP288 |
| A | GLY396 |
| A | HOH731 |
| B | TYR194 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | GLU192 |
| A | ASN193 |
| A | ALA262 |
| A | HIS263 |
| A | HOH638 |
| A | HOH885 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | ASN200 |
| A | GLN201 |
| A | ASP228 |
| A | THR229 |
| A | SER230 |
| A | ASN231 |
| A | HOH655 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | GLY167 |
| A | GLN168 |
| A | ARG171 |
| A | HOH604 |
| A | HOH608 |
| B | THR185 |
| B | GLU192 |
| B | HOH849 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | GLY320 |
| A | ASN405 |
| A | TYR406 |
| A | EDO510 |
| A | HOH611 |
| A | HOH640 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | ALA153 |
| A | LYS156 |
| A | HOH686 |
| B | GLU249 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | LYS166 |
| B | LEU245 |
| B | ILE258 |
| B | MET260 |
| B | HOH768 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 510 |
| Chain | Residue |
| A | TRP126 |
| A | GLY127 |
| A | THR128 |
| A | GLY320 |
| A | EDO507 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 511 |
| Chain | Residue |
| A | PRO421 |
| A | HOH896 |
| B | PRO421 |
| B | HOH646 |
| site_id | AD3 |
| Number of Residues | 22 |
| Details | binding site for residue SSA B 501 |
| Chain | Residue |
| B | HOH713 |
| B | HOH866 |
| B | THR237 |
| B | GLU239 |
| B | ARG268 |
| B | GLU270 |
| B | ILE282 |
| B | ARG283 |
| B | MET284 |
| B | PHE287 |
| B | LYS289 |
| B | GLU291 |
| B | GLU355 |
| B | ILE356 |
| B | SER357 |
| B | SER358 |
| B | ASN389 |
| B | SER391 |
| B | ALA394 |
| B | ARG397 |
| B | HOH601 |
| B | HOH630 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 B 502 |
| Chain | Residue |
| B | ARG276 |
| B | ASP277 |
| B | ARG283 |
| B | ARG354 |
| B | GLU355 |
| B | ARG397 |
| B | HOH616 |
| B | HOH642 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 503 |
| Chain | Residue |
| A | SER53 |
| A | LYS115 |
| B | VAL121 |
| B | GLU122 |
| B | HOH624 |
| B | HOH917 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 504 |
| Chain | Residue |
| B | LYS62 |
| B | THR141 |
| B | ARG279 |
| B | HOH690 |
| site_id | AD7 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| A | TYR194 |
| B | MET165 |
| B | HIS173 |
| B | MET284 |
| B | GLN286 |
| B | PHE287 |
| B | ASP288 |
| B | GLY396 |
| B | HOH760 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 506 |
| Chain | Residue |
| B | ASN200 |
| B | GLN201 |
| B | ASP228 |
| B | THR229 |
| B | SER230 |
| B | ASN231 |
| B | HOH669 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 507 |
| Chain | Residue |
| B | GLU192 |
| B | ASN193 |
| B | ALA262 |
| B | HIS263 |
| B | HOH641 |
| B | HOH916 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 508 |
| Chain | Residue |
| B | GLY320 |
| B | ASN405 |
| B | TYR406 |
| B | HOH645 |
| B | HOH656 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 509 |
| Chain | Residue |
| B | TRP126 |
| B | GLY127 |
| B | THR128 |
| B | GLY320 |
| B | PRO322 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 510 |
| Chain | Residue |
| B | PHE179 |
| B | GLU186 |
| B | GLN187 |
| B | TYR422 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 511 |
| Chain | Residue |
| B | LEU106 |
| B | ALA108 |
| B | CYS338 |
| B | TRP363 |
| B | HOH831 |
| site_id | AE5 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 512 |
| Chain | Residue |
| B | LYS17 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | THR237 | |
| B | SER391 | |
| A | ARG268 | |
| A | GLU291 | |
| A | GLU355 | |
| A | SER391 | |
| B | THR237 | |
| B | ARG268 | |
| B | GLU291 | |
| B | GLU355 |
