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 | 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 | 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 | 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 | 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 |