4Q15
Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with Halofuginone and AMPPNP in space group P212121 at 2.35 A
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 |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004827 | molecular_function | proline-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
B | 0006433 | biological_process | prolyl-tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 801 |
Chain | Residue |
A | ARG390 |
A | ANP802 |
A | HOH923 |
A | HOH924 |
A | HOH925 |
A | HOH1008 |
site_id | AC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ANP A 802 |
Chain | Residue |
A | ILE400 |
A | ARG401 |
A | THR402 |
A | PHE405 |
A | GLN475 |
A | ALA476 |
A | ALA477 |
A | THR512 |
A | ARG514 |
A | MG801 |
A | HFG803 |
A | HOH923 |
A | HOH924 |
A | HOH928 |
A | HOH942 |
A | HOH950 |
A | HOH1008 |
A | HOH1038 |
A | ARG390 |
A | GLU392 |
A | PHE399 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE HFG A 803 |
Chain | Residue |
A | PHE335 |
A | GLU338 |
A | VAL339 |
A | PRO358 |
A | THR359 |
A | GLU361 |
A | ARG390 |
A | TRP407 |
A | PHE454 |
A | THR478 |
A | HIS480 |
A | TRP509 |
A | GLY510 |
A | ANP802 |
A | HOH925 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 801 |
Chain | Residue |
B | ANP802 |
B | HOH930 |
B | HOH931 |
B | HOH932 |
B | HOH933 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ANP B 802 |
Chain | Residue |
B | ARG390 |
B | GLU392 |
B | LYS394 |
B | PHE399 |
B | ILE400 |
B | ARG401 |
B | THR402 |
B | PHE405 |
B | GLN475 |
B | ALA476 |
B | ALA477 |
B | THR512 |
B | ARG514 |
B | MG801 |
B | HFG803 |
B | HOH919 |
B | HOH930 |
B | HOH931 |
B | HOH933 |
B | HOH954 |
B | HOH960 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE HFG B 803 |
Chain | Residue |
B | PHE335 |
B | GLU338 |
B | VAL339 |
B | PRO358 |
B | THR359 |
B | GLU361 |
B | ARG390 |
B | TRP407 |
B | PHE454 |
B | THR478 |
B | HIS480 |
B | TRP509 |
B | GLY510 |
B | ANP802 |
B | HOH932 |
B | HOH1010 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 804 |
Chain | Residue |
B | GLU417 |
B | TYR481 |
B | GLY483 |
B | THR484 |
B | HIS505 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 805 |
Chain | Residue |
B | LYS567 |
B | GLN570 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 806 |
Chain | Residue |
B | LEU531 |
B | SER536 |
B | LYS537 |
B | TYR538 |
B | ILE595 |
B | HOH955 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|Ref.7, ECO:0007744|PDB:6T7K |
Chain | Residue | Details |
A | ARG390 | |
A | HIS480 | |
B | ARG390 | |
B | HIS480 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25817387, ECO:0000269|PubMed:27798837, ECO:0000269|Ref.4, ECO:0007744|PDB:4OLF, ECO:0007744|PDB:4Q15, ECO:0007744|PDB:4YDQ |
Chain | Residue | Details |
A | ARG401 | |
A | GLN475 | |
A | THR512 | |
B | ARG401 | |
B | GLN475 | |
B | THR512 |