3NRR
Co-crystal structure of dihydrofolate reductase-thymidylate synthase from Babesia bovis with dUMP, Raltitrexed and NADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0004799 | molecular_function | thymidylate synthase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006231 | biological_process | dTMP biosynthetic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| A | 0032259 | biological_process | methylation |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004146 | molecular_function | dihydrofolate reductase activity |
| B | 0004799 | molecular_function | thymidylate synthase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006231 | biological_process | dTMP biosynthetic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| B | 0032259 | biological_process | methylation |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 513 |
| Chain | Residue |
| A | ALA433 |
| A | HOH596 |
| A | HOH713 |
| A | HOH922 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAP A 515 |
| Chain | Residue |
| A | GLN28 |
| A | ILE29 |
| A | GLY66 |
| A | ARG67 |
| A | LYS68 |
| A | THR69 |
| A | LEU88 |
| A | SER89 |
| A | ARG90 |
| A | THR91 |
| A | GLU102 |
| A | LEU123 |
| A | GLY125 |
| A | SER126 |
| A | PHE127 |
| A | TYR129 |
| A | GLU131 |
| A | THR154 |
| A | D16520 |
| A | HOH640 |
| A | HOH716 |
| A | HOH734 |
| A | HOH801 |
| A | HOH822 |
| B | ARG305 |
| A | VAL15 |
| A | ALA16 |
| A | ILE23 |
| A | GLY24 |
| A | ASN27 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE D16 A 520 |
| Chain | Residue |
| A | PHE14 |
| A | VAL15 |
| A | ALA16 |
| A | ASP37 |
| A | PHE38 |
| A | ARG42 |
| A | PRO74 |
| A | SER77 |
| A | LEU123 |
| A | THR144 |
| A | NAP515 |
| A | HOH601 |
| A | HOH628 |
| A | HOH834 |
| A | HOH876 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE UMP A 525 |
| Chain | Residue |
| A | ARG248 |
| A | CYS393 |
| A | HIS394 |
| A | GLN412 |
| A | ARG413 |
| A | SER414 |
| A | ASP416 |
| A | GLY420 |
| A | ASN424 |
| A | HIS454 |
| A | TYR456 |
| A | D16530 |
| A | HOH559 |
| A | HOH603 |
| B | ARG373 |
| B | ARG374 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE D16 A 530 |
| Chain | Residue |
| A | SER281 |
| A | GLU285 |
| A | ILE306 |
| A | TRP307 |
| A | ASN310 |
| A | ASP416 |
| A | LEU419 |
| A | GLY420 |
| A | PHE423 |
| A | TYR456 |
| A | MET509 |
| A | SER510 |
| A | UMP525 |
| A | HOH556 |
| A | HOH593 |
| A | HOH603 |
| A | HOH631 |
| A | HOH849 |
| A | HOH879 |
| A | HOH914 |
| A | HOH1020 |
| A | HOH1029 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 531 |
| Chain | Residue |
| A | ILE356 |
| A | GLN358 |
| A | GLU361 |
| A | ILE362 |
| A | ILE376 |
| A | EDO533 |
| B | TRP380 |
| B | VAL382 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 532 |
| Chain | Residue |
| A | HOH833 |
| A | LYS214 |
| A | TYR215 |
| A | VAL216 |
| A | HOH755 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 533 |
| Chain | Residue |
| A | GLU361 |
| A | EDO531 |
| A | HOH1056 |
| B | LYS386 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 534 |
| Chain | Residue |
| A | PHE163 |
| A | LYS187 |
| A | HOH625 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 535 |
| Chain | Residue |
| A | VAL17 |
| A | LYS21 |
| A | PHE156 |
| A | PRO157 |
| A | HOH657 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 536 |
| Chain | Residue |
| A | TYR215 |
| A | LEU239 |
| A | TYR254 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 537 |
| Chain | Residue |
| A | ARG39 |
| A | PHE40 |
| A | ASN43 |
| A | HOH918 |
| B | LEU202 |
| B | THR206 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 540 |
| Chain | Residue |
| A | GLN437 |
| A | PRO481 |
| A | HOH542 |
| A | HOH596 |
| A | HOH688 |
| A | HOH1052 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 514 |
| Chain | Residue |
| A | ASP199 |
| B | GLU185 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 539 |
| Chain | Residue |
| A | GLU185 |
| B | ASP199 |
| B | HOH947 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 513 |
| Chain | Residue |
| A | ASN297 |
| B | ASN20 |
| B | PRO151 |
| B | GLY152 |
| B | TYR155 |
| site_id | BC8 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP B 515 |
| Chain | Residue |
| A | ARG305 |
| A | HOH617 |
| A | HOH1012 |
| B | VAL15 |
| B | ALA16 |
| B | ILE23 |
| B | GLY24 |
| B | HIS25 |
| B | ASN27 |
| B | GLN28 |
| B | ILE29 |
| B | GLY66 |
| B | ARG67 |
| B | LYS68 |
| B | THR69 |
| B | LEU88 |
| B | SER89 |
| B | ARG90 |
| B | THR91 |
| B | GLU102 |
| B | LEU123 |
| B | GLY125 |
| B | SER126 |
| B | PHE127 |
| B | TYR129 |
| B | GLU131 |
| B | THR154 |
| B | D16520 |
| B | HOH787 |
| B | HOH807 |
| B | HOH896 |
| site_id | BC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE D16 B 520 |
| Chain | Residue |
| B | PHE14 |
| B | VAL15 |
| B | ALA16 |
| B | HIS33 |
| B | ASP37 |
| B | PHE38 |
| B | ARG42 |
| B | SER77 |
| B | LEU123 |
| B | THR144 |
| B | NAP515 |
| B | HOH565 |
| B | HOH793 |
| site_id | CC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE UMP B 525 |
| Chain | Residue |
| A | ARG373 |
| A | ARG374 |
| B | ARG248 |
| B | CYS393 |
| B | HIS394 |
| B | GLN412 |
| B | ARG413 |
| B | SER414 |
| B | ASP416 |
| B | GLY420 |
| B | ASN424 |
| B | HIS454 |
| B | TYR456 |
| B | HOH526 |
| B | D16530 |
| B | HOH637 |
| site_id | CC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE D16 B 530 |
| Chain | Residue |
| B | ALA278 |
| B | SER281 |
| B | GLU285 |
| B | ILE306 |
| B | TRP307 |
| B | ASN310 |
| B | ASP416 |
| B | LEU419 |
| B | GLY420 |
| B | PHE423 |
| B | TYR456 |
| B | MET509 |
| B | SER510 |
| B | ALA511 |
| B | HOH516 |
| B | HOH523 |
| B | UMP525 |
| B | HOH548 |
| B | HOH672 |
| B | HOH685 |
| B | HOH695 |
| B | HOH757 |
| B | HOH982 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 532 |
| Chain | Residue |
| A | TRP380 |
| A | VAL382 |
| B | GLN358 |
| B | GLU361 |
| B | ILE376 |
| B | HOH709 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 533 |
| Chain | Residue |
| B | LYS214 |
| B | TYR215 |
| B | LEU239 |
| B | TYR254 |
| B | HOH899 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 534 |
| Chain | Residue |
| B | ILE159 |
| B | PRO160 |
| B | PHE163 |
| B | TYR184 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 537 |
| Chain | Residue |
| B | THR106 |
| B | ARG109 |
| B | ASP110 |
Functional Information from PROSITE/UniProt
| site_id | PS00091 |
| Number of Residues | 29 |
| Details | THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrlIvcsWNvsdlkkma.....LpPCHcffQFyV |
| Chain | Residue | Details |
| A | ARG373-VAL401 |
