4WI1
Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with TCMDC-124506
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 | 12 |
| Details | binding site for residue 3O6 A 801 |
| Chain | Residue |
| A | TYR266 |
| A | ILE518 |
| A | ILE520 |
| A | MET521 |
| A | TYR285 |
| A | ALA291 |
| A | ARG403 |
| A | GLU404 |
| A | ILE474 |
| A | THR513 |
| A | ILE516 |
| A | GLY517 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 802 |
| Chain | Residue |
| A | HIS248 |
| A | TYR585 |
| A | HIS589 |
| A | ARG593 |
| A | HOH1146 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 803 |
| Chain | Residue |
| A | ALA290 |
| A | SER536 |
| A | LYS537 |
| A | TYR538 |
| A | HOH993 |
| A | HOH1043 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 804 |
| Chain | Residue |
| A | LEU309 |
| A | ASN310 |
| A | LYS381 |
| A | HOH1013 |
| A | HOH1131 |
| A | HOH1231 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 805 |
| Chain | Residue |
| A | PRO717 |
| A | LEU718 |
| A | ARG738 |
| A | HOH1242 |
| A | HOH1258 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 806 |
| Chain | Residue |
| A | PHE459 |
| A | EDO807 |
| A | HOH1085 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 807 |
| Chain | Residue |
| A | GLU417 |
| A | VAL421 |
| A | PHE459 |
| A | TYR547 |
| A | LYS548 |
| A | EDO806 |
| A | HOH936 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 808 |
| Chain | Residue |
| A | LYS258 |
| A | GLU469 |
| A | THR522 |
| A | HIS523 |
| A | GLY524 |
| A | LYS651 |
| A | HOH1300 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 809 |
| Chain | Residue |
| A | THR362 |
| A | GLN384 |
| A | ASN386 |
| A | GLU409 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue IMD A 810 |
| Chain | Residue |
| A | LYS448 |
| A | PHE454 |
| A | GLN475 |
| A | THR478 |
| A | HIS480 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 811 |
| Chain | Residue |
| A | MET364 |
| A | TYR365 |
| A | SER366 |
| B | ASP280 |
| B | ILE281 |
| site_id | AD3 |
| Number of Residues | 13 |
| Details | binding site for residue 3O6 B 801 |
| Chain | Residue |
| B | TYR266 |
| B | TYR285 |
| B | LEU287 |
| B | ALA291 |
| B | ARG403 |
| B | GLU404 |
| B | ILE474 |
| B | THR513 |
| B | ILE516 |
| B | ILE518 |
| B | ILE520 |
| B | MET521 |
| B | EDO804 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 802 |
| Chain | Residue |
| B | ASP525 |
| B | LYS527 |
| B | ASP617 |
| B | ASN619 |
| B | GLU688 |
| B | EDO807 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 803 |
| Chain | Residue |
| B | SER536 |
| B | LYS537 |
| B | TYR538 |
| B | ILE595 |
| B | HOH967 |
| B | HOH982 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 804 |
| Chain | Residue |
| B | SER263 |
| B | TYR746 |
| B | 3O6801 |
| B | HOH1028 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 805 |
| Chain | Residue |
| B | HIS505 |
| B | GLU417 |
| B | ASN458 |
| B | TYR481 |
| B | GLY483 |
| B | THR484 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 806 |
| Chain | Residue |
| B | LYS258 |
| B | GLU469 |
| B | HIS523 |
| B | GLY524 |
| B | LYS651 |
| B | HOH1137 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 807 |
| Chain | Residue |
| B | ASP525 |
| B | ASP526 |
| B | EDO802 |
| B | HOH1029 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 808 |
| Chain | Residue |
| B | PRO717 |
| B | GLN720 |
| B | ARG738 |
| B | HOH1227 |
| B | HOH1252 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue IMD B 809 |
| Chain | Residue |
| B | TYR279 |
| B | TYR279 |
| B | ASP280 |
| B | ASP280 |
| B | GLU392 |
| B | GLU392 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25817387","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27798837","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2014","submissionDatabase":"PDB data bank","title":"Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase)from Plasmodium falciparum in complex with Halofuginone and AMPPNP.","authors":["Dranow D.M.","Edwards T.E.","Lorimer D."]}},{"source":"PDB","id":"4OLF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Q15","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YDQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2019","submissionDatabase":"PDB data bank","title":"Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with NCP-26 and L-Proline.","authors":["Johansson C.","Wang J.","Tye M.","Payne N.C.","Mazitschek R.","Thompson A.","Arrowsmith C.H.","Bountra C.","Edwards A.","Oppermann U.C.T."]}},{"source":"PDB","id":"6T7K","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
