4NCX
Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum 3D7
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 | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 801 |
| Chain | Residue |
| A | ALA290 |
| A | SER536 |
| A | LYS537 |
| A | TYR538 |
| A | ILE595 |
| A | HOH938 |
| A | HOH1029 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 802 |
| Chain | Residue |
| A | LYS422 |
| A | HOH962 |
| A | HOH990 |
| A | HOH1015 |
| A | HOH1133 |
| A | HOH1207 |
| A | LEU309 |
| A | LYS381 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 803 |
| Chain | Residue |
| A | GLN475 |
| A | THR478 |
| A | GLY510 |
| A | ARG514 |
| A | HOH934 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 804 |
| Chain | Residue |
| A | GLU312 |
| A | HOH915 |
| A | HOH1063 |
| B | PRO289 |
| B | ALA290 |
| B | TYR293 |
| B | LYS537 |
| B | EDO801 |
| B | HOH1134 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 805 |
| Chain | Residue |
| A | THR321 |
| B | PHE393 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 806 |
| Chain | Residue |
| A | PRO533 |
| A | HOH1034 |
| A | HOH1056 |
| A | HOH1098 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 801 |
| Chain | Residue |
| A | EDO804 |
| A | HOH967 |
| B | SER536 |
| B | LYS537 |
| B | TYR538 |
| B | ILE595 |
| B | HOH1134 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 802 |
| Chain | Residue |
| B | ASP525 |
| B | LYS527 |
| B | ASP617 |
| B | ASN619 |
| B | GLU688 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| 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 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| 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 |
