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 | 24 |
| 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 | 4 |
| 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 |
