4K87
Crystal structure of human prolyl-tRNA synthetase (substrate bound form)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004827 | molecular_function | proline-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
A | 0006433 | biological_process | prolyl-tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 601 |
Chain | Residue |
A | CYS448 |
A | CYS453 |
A | CYS495 |
A | CYS497 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ADN A 602 |
Chain | Residue |
A | GLN237 |
A | GLY239 |
A | THR240 |
A | GLY274 |
A | THR276 |
A | ARG278 |
A | PRO603 |
A | HOH764 |
A | ARG152 |
A | PHE161 |
A | LEU162 |
A | ARG163 |
A | THR164 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PRO A 603 |
Chain | Residue |
A | THR121 |
A | GLU123 |
A | ARG152 |
A | TRP169 |
A | GLU171 |
A | HIS173 |
A | PHE216 |
A | HIS242 |
A | SER272 |
A | TRP273 |
A | ADN602 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24100331, ECO:0007744|PDB:4K87 |
Chain | Residue | Details |
A | THR121 | |
A | ARG152 | |
A | HIS242 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331, ECO:0000269|PubMed:37212275, ECO:0007744|PDB:4HVC, ECO:0007744|PDB:4K87, ECO:0007744|PDB:7Y1H, ECO:0007744|PDB:7Y1W, ECO:0007744|PDB:7Y28, ECO:0007744|PDB:7Y3S |
Chain | Residue | Details |
A | GLU154 | |
A | ARG163 | |
A | THR164 | |
A | THR240 | |
A | THR276 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:37212275, ECO:0007744|PDB:7Y1H, ECO:0007744|PDB:7Y1W, ECO:0007744|PDB:7Y28, ECO:0007744|PDB:7Y3S |
Chain | Residue | Details |
A | GLN237 | |
A | ARG278 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331, ECO:0000269|PubMed:37212275, ECO:0007744|PDB:4HVC, ECO:0007744|PDB:4K86, ECO:0007744|PDB:4K87, ECO:0007744|PDB:7Y1H, ECO:0007744|PDB:7Y1W, ECO:0007744|PDB:7Y28, ECO:0007744|PDB:7Y3S |
Chain | Residue | Details |
A | CYS448 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331, ECO:0000269|PubMed:37212275, ECO:0007744|PDB:4HVC, ECO:0007744|PDB:4K86, ECO:0007744|PDB:4K87, ECO:0007744|PDB:4K88, ECO:0007744|PDB:7Y1H, ECO:0007744|PDB:7Y1W, ECO:0007744|PDB:7Y28, ECO:0007744|PDB:7Y3S |
Chain | Residue | Details |
A | CYS453 | |
A | CYS495 | |
A | CYS497 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | SER0 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
A | ARG152 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER350 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS503 |