Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004828 | molecular_function | serine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006434 | biological_process | seryl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004828 | molecular_function | serine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006434 | biological_process | seryl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AMP A1507 |
| Chain | Residue |
| A | ARG256 |
| A | HIS347 |
| A | SER348 |
| A | THR380 |
| A | HOH3431 |
| A | HOH3450 |
| A | HOH3453 |
| A | GLU258 |
| A | MET270 |
| A | ARG271 |
| A | VAL272 |
| A | PHE275 |
| A | LYS277 |
| A | GLU345 |
| A | THR346 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AMP B1508 |
| Chain | Residue |
| B | ARG256 |
| B | GLU258 |
| B | MET270 |
| B | ARG271 |
| B | VAL272 |
| B | PHE275 |
| B | LYS277 |
| B | GLU345 |
| B | THR346 |
| B | HIS347 |
| B | SER348 |
| B | THR380 |
| B | ARG386 |
| B | HOH3457 |
| B | HOH3458 |
| B | HOH3471 |
| B | HOH3472 |
| B | HOH3474 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00176","evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ses |
| Chain | Residue | Details |
| A | ASP265 | |
| A | GLU258 | |
| A | SER261 | |
| A | ARG256 | |
| A | ARG271 | |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ses |
| Chain | Residue | Details |
| B | ASP265 | |
| B | GLU258 | |
| B | SER261 | |
| B | ARG256 | |
| B | ARG271 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ses |
| Chain | Residue | Details |
| A | ARG256 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ses |
| Chain | Residue | Details |
| B | ARG256 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 884 |
| Chain | Residue | Details |
| A | ARG256 | electrostatic stabiliser |
| A | ARG271 | electrostatic stabiliser |
| A | GLU345 | metal ligand |
| A | SER348 | metal ligand |
| A | ARG386 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 884 |
| Chain | Residue | Details |
| B | ARG256 | electrostatic stabiliser |
| B | ARG271 | electrostatic stabiliser |
| B | GLU345 | metal ligand |
| B | SER348 | metal ligand |
| B | ARG386 | electrostatic stabiliser |
