3K2H
Co-crystal structure of dihydrofolate reductase/thymidylate synthase from Babesia bovis with dUMP, Pemetrexed 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 | 17 |
| Details | BINDING SITE FOR RESIDUE UMP A 512 |
| Chain | Residue |
| A | ARG248 |
| A | ASN424 |
| A | HIS454 |
| A | TYR456 |
| A | LYA513 |
| A | HOH566 |
| A | HOH730 |
| B | ARG373 |
| B | ARG374 |
| A | LEU390 |
| A | CYS393 |
| A | HIS394 |
| A | GLN412 |
| A | ARG413 |
| A | SER414 |
| A | CYS415 |
| A | ASP416 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE LYA A 513 |
| Chain | Residue |
| A | ALA278 |
| A | SER281 |
| A | ILE306 |
| A | ASN310 |
| A | LEU390 |
| A | ASP416 |
| A | LEU419 |
| A | GLY420 |
| A | PHE423 |
| A | TYR456 |
| A | MET509 |
| A | SER510 |
| A | UMP512 |
| A | HOH559 |
| A | HOH653 |
| A | HOH690 |
| A | HOH694 |
| A | HOH710 |
| A | HOH735 |
| A | HOH794 |
| A | HOH843 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE LYA A 514 |
| Chain | Residue |
| A | PHE14 |
| A | VAL15 |
| A | ALA16 |
| A | ASP37 |
| A | PHE38 |
| A | ARG39 |
| A | LEU41 |
| A | ARG42 |
| A | SER77 |
| A | ARG83 |
| A | LEU123 |
| A | TYR129 |
| A | THR144 |
| A | NAP515 |
| A | HOH571 |
| A | HOH575 |
| A | HOH608 |
| A | HOH664 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP A 515 |
| Chain | Residue |
| A | VAL15 |
| A | ALA16 |
| A | ILE23 |
| A | GLY24 |
| A | HIS25 |
| A | ASN27 |
| A | GLN28 |
| A | ILE29 |
| A | TRP31 |
| A | GLY66 |
| A | ARG67 |
| A | LYS68 |
| A | THR69 |
| A | SER72 |
| A | LEU88 |
| A | SER89 |
| A | ARG90 |
| A | THR91 |
| A | GLU102 |
| A | ASP103 |
| A | LEU104 |
| A | LEU123 |
| A | GLY125 |
| A | SER126 |
| A | PHE127 |
| A | TYR129 |
| A | GLU131 |
| A | THR154 |
| A | LYA514 |
| A | HOH587 |
| A | HOH721 |
| B | ARG305 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 516 |
| Chain | Residue |
| A | GLN358 |
| A | GLU361 |
| A | ILE376 |
| A | HOH858 |
| B | TRP380 |
| B | VAL382 |
| B | LEU385 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 517 |
| Chain | Residue |
| B | GLN358 |
| B | GLU361 |
| B | ILE362 |
| B | ILE376 |
| B | HOH622 |
| A | TRP380 |
| A | VAL382 |
| A | LEU385 |
| B | ILE356 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 517 |
| Chain | Residue |
| A | ARG374 |
| B | ASN319 |
| B | ALA389 |
| B | PRO391 |
| B | HOH691 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE UMP B 512 |
| Chain | Residue |
| A | ARG373 |
| A | ARG374 |
| B | ARG248 |
| B | LEU390 |
| B | CYS393 |
| B | HIS394 |
| B | GLN412 |
| B | ARG413 |
| B | SER414 |
| B | CYS415 |
| B | ASP416 |
| B | ASN424 |
| B | HIS454 |
| B | TYR456 |
| B | LYA513 |
| B | HOH544 |
| B | HOH717 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE LYA B 513 |
| Chain | Residue |
| B | ALA278 |
| B | SER281 |
| B | ILE306 |
| B | ASN310 |
| B | LEU390 |
| B | ASP416 |
| B | LEU419 |
| B | GLY420 |
| B | PHE423 |
| B | MET509 |
| B | SER510 |
| B | UMP512 |
| B | HOH524 |
| B | HOH545 |
| B | HOH552 |
| B | HOH556 |
| B | HOH566 |
| B | HOH595 |
| B | HOH718 |
| B | HOH737 |
| B | HOH763 |
| B | HOH804 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE LYA B 514 |
| Chain | Residue |
| B | PHE14 |
| B | VAL15 |
| B | ALA16 |
| B | ASP37 |
| B | PHE38 |
| B | ARG39 |
| B | LEU41 |
| B | ARG42 |
| B | LEU80 |
| B | ARG83 |
| B | LEU123 |
| B | THR144 |
| B | NAP515 |
| B | HOH534 |
| B | HOH629 |
| B | HOH713 |
| site_id | BC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP B 515 |
| Chain | Residue |
| A | ARG305 |
| B | VAL15 |
| B | ALA16 |
| B | ILE23 |
| B | GLY24 |
| B | ASN27 |
| B | GLN28 |
| B | ILE29 |
| B | TRP31 |
| B | GLY66 |
| B | ARG67 |
| B | LYS68 |
| B | THR69 |
| B | SER72 |
| B | LEU88 |
| B | SER89 |
| B | ARG90 |
| B | THR91 |
| B | GLU102 |
| B | ASP103 |
| B | LEU123 |
| B | GLY125 |
| B | SER126 |
| B | PHE127 |
| B | TYR129 |
| B | GLU131 |
| B | THR154 |
| B | LYA514 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 516 |
| Chain | Residue |
| A | ARG248 |
| A | ALA389 |
| A | PRO391 |
| A | HOH820 |
| B | ARG374 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 518 |
| Chain | Residue |
| A | PHE340 |
| A | GLY341 |
| A | ASN381 |
| A | SER383 |
| B | PHE340 |
| B | GLY341 |
| B | ASN381 |
| B | SER383 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| A | CYS393 | |
| A | SER427 | |
| A | ASN424 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| B | CYS393 | |
| B | SER427 | |
| B | ASN424 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| A | ASP37 | |
| A | ILE29 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| B | ASP37 | |
| B | ILE29 |
| site_id | CSA5 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| A | ASP452 | |
| A | HIS454 | |
| A | GLU285 | |
| A | SER414 | |
| A | ASP416 | |
| A | CYS393 |
| site_id | CSA6 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| B | ASP452 | |
| B | HIS454 | |
| B | GLU285 | |
| B | SER414 | |
| B | ASP416 | |
| B | CYS393 |
