5V58
Crystal structure of human prolyl-tRNA synthetase in complex with Aze-SA
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 | 16 |
Details | binding site for residue 8X1 A 1601 |
Chain | Residue |
A | THR1121 |
A | GLN1237 |
A | GLY1239 |
A | THR1240 |
A | HIS1242 |
A | GLY1274 |
A | THR1276 |
A | ARG1278 |
A | GLU1123 |
A | ARG1152 |
A | GLU1154 |
A | PHE1161 |
A | LEU1162 |
A | THR1164 |
A | PHE1167 |
A | TRP1169 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue ZN A 1602 |
Chain | Residue |
A | CYS1448 |
A | CYS1453 |
A | CYS1495 |
A | CYS1497 |
A | ASN1500 |
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 | THR1121 | |
A | ARG1152 | |
A | HIS1242 |
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 | GLU1154 | |
A | ARG1163 | |
A | THR1164 | |
A | THR1240 | |
A | THR1276 |
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 | GLN1237 | |
A | ARG1278 |
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 | CYS1448 |
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 | CYS1453 | |
A | CYS1495 | |
A | CYS1497 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
A | ARG1152 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER1350 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS1503 |