4TWA
Crystal Structure of Prolyl-tRNA Synthetase (PRS) from Plasmodium falciparum
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 | 2 |
| Details | binding site for residue CL A 801 |
| Chain | Residue |
| A | ARG403 |
| A | CL802 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 802 |
| Chain | Residue |
| A | LYS394 |
| A | ARG401 |
| A | CL801 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 803 |
| Chain | Residue |
| A | ASN310 |
| A | LYS381 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 804 |
| Chain | Residue |
| A | PHE393 |
| A | ARG403 |
| A | ARG695 |
| A | LYS324 |
| A | ARG390 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 805 |
| Chain | Residue |
| A | ASP429 |
| A | ARG432 |
| A | LYS445 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 806 |
| Chain | Residue |
| A | ASN458 |
| A | LYS548 |
| A | PRO603 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 807 |
| Chain | Residue |
| A | TYR293 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 808 |
| Chain | Residue |
| A | ARG432 |
| A | GLU436 |
| A | GLU437 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 809 |
| Chain | Residue |
| A | ASN618 |
| A | LYS647 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 801 |
| Chain | Residue |
| B | CL802 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 802 |
| Chain | Residue |
| B | LYS394 |
| B | GLN395 |
| B | ARG401 |
| B | CL801 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 803 |
| Chain | Residue |
| B | ASN310 |
| B | LYS381 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 804 |
| Chain | Residue |
| A | ARG578 |
| A | ALA579 |
| A | SER580 |
| A | PRO722 |
| B | TYR375 |
| B | ARG376 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 805 |
| Chain | Residue |
| B | ASN618 |
| B | ASN643 |
| B | LYS647 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 806 |
| Chain | Residue |
| A | LYS307 |
| B | TYR293 |
| B | LYS537 |
| B | LYS539 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 807 |
| Chain | Residue |
| B | ASN623 |
| B | ARG695 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 808 |
| Chain | Residue |
| B | LYS344 |
| B | TYR345 |
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 |
