1JTU
E. coli Thymidylate Synthase in a Complex with dUMP and LY338913, A Polyglutamylated Pyrrolo(2,3-d)pyrimidine-based Antifolate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004799 | molecular_function | thymidylate synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006231 | biological_process | dTMP biosynthetic process |
| A | 0006235 | biological_process | dTTP biosynthetic process |
| A | 0006417 | biological_process | regulation of translation |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0009314 | biological_process | response to radiation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| A | 0032259 | biological_process | methylation |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004799 | molecular_function | thymidylate synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006231 | biological_process | dTMP biosynthetic process |
| B | 0006235 | biological_process | dTTP biosynthetic process |
| B | 0006417 | biological_process | regulation of translation |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0009314 | biological_process | response to radiation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| B | 0032259 | biological_process | methylation |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE UMP A 565 |
| Chain | Residue |
| A | ARG21 |
| A | ASN177 |
| A | HIS207 |
| A | TYR209 |
| A | LYB501 |
| A | HOH644 |
| A | HOH647 |
| B | ARG126 |
| B | ARG127 |
| A | TYR94 |
| A | CYS146 |
| A | HIS147 |
| A | GLN165 |
| A | ARG166 |
| A | SER167 |
| A | CYS168 |
| A | ASP169 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE LYB A 501 |
| Chain | Residue |
| A | HIS51 |
| A | ARG53 |
| A | ILE79 |
| A | TRP83 |
| A | LEU143 |
| A | ASP169 |
| A | GLY173 |
| A | PHE176 |
| A | VAL262 |
| A | ALA263 |
| A | UMP565 |
| A | HOH652 |
| A | HOH664 |
| A | HOH682 |
| A | HOH684 |
| A | HOH699 |
| A | HOH739 |
| A | HOH742 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE UMP B 565 |
| Chain | Residue |
| A | ARG126 |
| A | ARG127 |
| B | ARG21 |
| B | CYS146 |
| B | HIS147 |
| B | GLN165 |
| B | ARG166 |
| B | SER167 |
| B | CYS168 |
| B | ASP169 |
| B | ASN177 |
| B | HIS207 |
| B | TYR209 |
| B | LYB502 |
| B | HOH714 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE LYB B 502 |
| Chain | Residue |
| B | HIS51 |
| B | THR78 |
| B | ILE79 |
| B | TRP80 |
| B | TRP83 |
| B | ASP169 |
| B | GLY173 |
| B | PHE176 |
| B | ALA263 |
| B | UMP565 |
| B | HOH666 |
| B | HOH676 |
| B | HOH741 |
| B | HOH745 |
| B | HOH775 |
| B | HOH787 |
| B | HOH804 |
| B | HOH829 |
Functional Information from PROSITE/UniProt
| site_id | PS00091 |
| Number of Residues | 29 |
| Details | THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriIvsaWNvgeldkma.....LaPCHaffQFyV |
| Chain | Residue | Details |
| A | ARG126-VAL154 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00008, ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0000269|PubMed:9416600 |
| Chain | Residue | Details |
| A | CYS146 | |
| B | CYS146 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC |
| Chain | Residue | Details |
| A | ARG21 | |
| A | ARG166 | |
| A | ASN177 | |
| A | HIS207 | |
| B | ARG21 | |
| B | ARG166 | |
| B | ASN177 | |
| B | HIS207 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:8312270, ECO:0007744|PDB:1TYS |
| Chain | Residue | Details |
| A | HIS51 | |
| A | ASP169 | |
| A | ALA263 | |
| B | HIS51 | |
| B | ASP169 | |
| B | ALA263 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:8973201, ECO:0007744|PDB:1KCE, ECO:0007744|PDB:2TSC |
| Chain | Residue | Details |
| A | ARG126 | |
| B | ARG126 |
