1SET
CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE
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 | 0004828 | molecular_function | serine-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 | 0006434 | biological_process | seryl-tRNA aminoacylation |
A | 0016260 | biological_process | selenocysteine biosynthetic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0070905 | molecular_function | serine binding |
B | 0000049 | molecular_function | tRNA binding |
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 | 0005737 | cellular_component | cytoplasm |
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 | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0070905 | molecular_function | serine binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SSA A 422 |
Chain | Residue |
A | THR225 |
A | GLU279 |
A | GLU345 |
A | THR346 |
A | HIS347 |
A | SER348 |
A | ASN378 |
A | THR380 |
A | ALA383 |
A | HOH427 |
A | HOH459 |
A | GLU227 |
A | HOH502 |
A | ARG256 |
A | GLU258 |
A | MET270 |
A | ARG271 |
A | VAL272 |
A | PHE275 |
A | LYS277 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE SSA B 423 |
Chain | Residue |
B | THR225 |
B | GLU227 |
B | ARG256 |
B | GLU258 |
B | MET270 |
B | ARG271 |
B | VAL272 |
B | PHE275 |
B | GLU279 |
B | GLU345 |
B | THR346 |
B | HIS347 |
B | SER348 |
B | ASN378 |
B | THR380 |
B | HOH469 |
B | HOH477 |
B | HOH478 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
A | THR225 | |
B | GLU279 | |
B | GLU345 | |
B | THR380 | |
A | ARG256 | |
A | VAL272 | |
A | GLU279 | |
A | GLU345 | |
A | THR380 | |
B | THR225 | |
B | ARG256 | |
B | VAL272 |
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 |