2H2Q
Crystal structure of Trypanosoma cruzi Dihydrofolate Reductase-Thymidylate synthase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 23 |
| Details | BINDING SITE FOR RESIDUE NAP A 523 |
| Chain | Residue |
| A | ALA28 |
| A | LYS79 |
| A | THR80 |
| A | LEU99 |
| A | SER100 |
| A | SER101 |
| A | THR102 |
| A | GLY130 |
| A | GLY131 |
| A | ILE154 |
| A | GLY155 |
| A | ILE35 |
| A | GLY156 |
| A | GLY157 |
| A | SER158 |
| A | TYR160 |
| A | ASP37 |
| A | GLY38 |
| A | ARG39 |
| A | SER40 |
| A | ILE41 |
| A | GLY77 |
| A | ARG78 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DU A 611 |
| Chain | Residue |
| A | CYS403 |
| A | HIS404 |
| A | GLN422 |
| A | ARG423 |
| A | SER424 |
| A | ASP426 |
| A | GLY430 |
| A | ASN434 |
| A | HIS464 |
| A | TYR466 |
| B | ARG383 |
| B | ARG384 |
| B | HOH655 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAP B 524 |
| Chain | Residue |
| B | ALA28 |
| B | ILE35 |
| B | GLY77 |
| B | ARG78 |
| B | LYS79 |
| B | THR80 |
| B | SER83 |
| B | LEU99 |
| B | SER100 |
| B | SER101 |
| B | THR102 |
| B | GLY130 |
| B | GLY131 |
| B | ILE154 |
| B | GLY156 |
| B | GLY157 |
| B | SER158 |
| B | TYR160 |
| B | HOH701 |
| B | HOH751 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DU B 612 |
| Chain | Residue |
| A | ARG383 |
| A | ARG384 |
| B | CYS403 |
| B | HIS404 |
| B | GLN422 |
| B | ARG423 |
| B | SER424 |
| B | ASP426 |
| B | GLY430 |
| B | ASN434 |
| B | HIS464 |
| B | TYR466 |
| B | HOH651 |
| B | HOH744 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 23 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGdgrsIPWnvpe.DmkfFrdvT |
| Chain | Residue | Details |
| A | GLY34-THR56 |
| site_id | PS00091 |
| Number of Residues | 29 |
| Details | THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrmLftaWNpsalprma.....LpPCHllaQFyV |
| Chain | Residue | Details |
| A | ARG383-VAL411 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS403 | |
| B | CYS403 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | VAL26 | |
| A | THR178 | |
| A | ARG257 | |
| A | HIS404 | |
| A | GLN422 | |
| A | ASN434 | |
| A | HIS464 | |
| B | VAL26 | |
| B | ALA28 | |
| B | GLY34 | |
| B | ASP48 | |
| A | ALA28 | |
| B | ARG78 | |
| B | LEU99 | |
| B | ILE154 | |
| B | GLY155 | |
| B | TYR160 | |
| B | THR178 | |
| B | ARG257 | |
| B | HIS404 | |
| B | GLN422 | |
| B | ASN434 | |
| A | GLY34 | |
| B | HIS464 | |
| A | ASP48 | |
| A | ARG78 | |
| A | LEU99 | |
| A | ILE154 | |
| A | GLY155 | |
| A | TYR160 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| A | CYS403 | |
| A | ASN434 | |
| A | SER437 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| B | CYS403 | |
| B | ASN434 | |
| B | SER437 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| A | ASP48 | |
| A | ILE41 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| B | ASP48 |
| site_id | CSA5 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| A | ASP426 | |
| A | ASP462 | |
| A | CYS403 | |
| A | HIS464 | |
| A | SER424 | |
| A | GLU295 |
| site_id | CSA6 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| B | ASP426 | |
| B | ASP462 | |
| B | CYS403 | |
| B | HIS464 | |
| B | SER424 | |
| B | GLU295 |
