5IFU
Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with Glyburide
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 GBM A 801 |
| Chain | Residue |
| A | TYR266 |
| A | ILE276 |
| A | GLU404 |
| A | ARG514 |
| A | GLY517 |
| A | TYR746 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 802 |
| Chain | Residue |
| B | ASP280 |
| B | ILE281 |
| A | MET364 |
| A | TYR365 |
| A | SER366 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue FMT A 803 |
| Chain | Residue |
| A | SER536 |
| A | LYS537 |
| A | TYR538 |
| A | ILE595 |
| A | HOH909 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue FMT A 804 |
| Chain | Residue |
| A | TYR278 |
| A | THR402 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 805 |
| Chain | Residue |
| A | LYS445 |
| A | HOH1044 |
| A | HOH1045 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue FMT A 806 |
| Chain | Residue |
| A | SER468 |
| A | SER655 |
| A | LYS672 |
| A | LYS673 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue FMT A 807 |
| Chain | Residue |
| A | CYS622 |
| A | GLU632 |
| A | HOH963 |
| A | HOH1040 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 808 |
| Chain | Residue |
| A | PRO725 |
| A | ASN726 |
| A | ARG738 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 809 |
| Chain | Residue |
| A | PRO724 |
| A | PRO725 |
| A | ASN726 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 810 |
| Chain | Residue |
| A | GLU404 |
| A | THR512 |
| A | ARG514 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 811 |
| Chain | Residue |
| A | GLN658 |
| A | MET727 |
| A | HOH924 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue FMT A 812 |
| Chain | Residue |
| A | ASP719 |
| A | HOH952 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 813 |
| Chain | Residue |
| A | GLU296 |
| A | GLN299 |
| A | ALA300 |
| A | ASN303 |
| A | HOH966 |
| B | EDO806 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue GBM B 801 |
| Chain | Residue |
| B | TYR266 |
| B | ILE276 |
| B | GLU404 |
| B | THR513 |
| B | ARG514 |
| B | GLY517 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue FMT B 802 |
| Chain | Residue |
| B | SER536 |
| B | LYS537 |
| B | TYR538 |
| B | HOH912 |
| site_id | AD7 |
| Number of Residues | 1 |
| Details | binding site for residue FMT B 803 |
| Chain | Residue |
| B | TYR278 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue FMT B 804 |
| Chain | Residue |
| A | GLN299 |
| A | ASN303 |
| B | TYR292 |
| B | GLN299 |
| B | HOH909 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue FMT B 805 |
| Chain | Residue |
| B | THR512 |
| B | ARG514 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 806 |
| Chain | Residue |
| A | EDO813 |
| B | GLU296 |
| B | GLN299 |
| B | ALA300 |
| B | ASN303 |
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 |
