3KJR
Crystal structure of dihydrofolate reductase/thymidylate synthase from Babesia bovis determined using SlipChip based microfluidics
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 | 31 |
| Details | BINDING SITE FOR RESIDUE NAP A 512 |
| Chain | Residue |
| A | VAL15 |
| A | LYS68 |
| A | THR69 |
| A | LEU88 |
| A | SER89 |
| A | ARG90 |
| A | THR91 |
| A | GLU102 |
| A | ASP103 |
| A | LEU104 |
| A | LEU123 |
| A | ALA16 |
| A | GLY124 |
| A | GLY125 |
| A | SER126 |
| A | PHE127 |
| A | LEU128 |
| A | TYR129 |
| A | GLU131 |
| A | THR154 |
| A | HOH700 |
| A | HOH797 |
| A | ILE23 |
| A | HOH918 |
| A | HOH1017 |
| A | GLY24 |
| A | ASN27 |
| A | GLN28 |
| A | ILE29 |
| A | GLY66 |
| A | ARG67 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP B 512 |
| Chain | Residue |
| B | VAL15 |
| B | ALA16 |
| B | ILE23 |
| B | GLY24 |
| B | HIS25 |
| B | ASN27 |
| B | GLN28 |
| B | ILE29 |
| B | TRP31 |
| B | GLY66 |
| B | ARG67 |
| B | LYS68 |
| B | THR69 |
| B | LEU88 |
| B | SER89 |
| B | ARG90 |
| B | THR91 |
| B | LEU123 |
| B | GLY124 |
| B | GLY125 |
| B | SER126 |
| B | PHE127 |
| B | LEU128 |
| B | TYR129 |
| B | GLU131 |
| B | THR154 |
| B | HOH849 |
| B | HOH856 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NHE A 513 |
| Chain | Residue |
| A | HIS36 |
| A | PHE172 |
| A | SER173 |
| A | THR174 |
| A | ASP175 |
| A | SER266 |
| A | ARG267 |
| A | HOH861 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 514 |
| Chain | Residue |
| A | LYS214 |
| A | TYR215 |
| A | VAL216 |
| A | THR464 |
| A | HOH710 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 515 |
| Chain | Residue |
| A | GLU284 |
| A | LEU287 |
| A | LYS302 |
| A | THR490 |
| A | ILE491 |
| A | HOH931 |
| A | HOH1044 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 516 |
| Chain | Residue |
| A | GLU285 |
| A | ILE306 |
| A | TRP307 |
| A | ASN310 |
| A | MET509 |
| A | HOH864 |
| A | HOH888 |
| A | HOH947 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 513 |
| Chain | Residue |
| B | VAL17 |
| B | ALA18 |
| B | LEU19 |
| B | LEU146 |
| B | HOH682 |
| B | HOH720 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 517 |
| Chain | Residue |
| A | VAL17 |
| A | ALA18 |
| A | LEU19 |
| A | LEU146 |
| A | HOH778 |
| A | HOH950 |
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 |
