6AOH
Crystal structure of Toxoplasma gondii TS-DHFR complexed with NADPH, dUMP, PDDF, and 5-(4-(3-(2-methoxypyrimidin-5-yl)phenyl)piperazin-1-yl)pyrimidine-2,4-diamine (TRC-2533)
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 | 14 |
| Details | binding site for residue UMP A 701 |
| Chain | Residue |
| A | ARG344 |
| A | HIS551 |
| A | TYR553 |
| A | CB3703 |
| B | ARG469 |
| B | ARG470 |
| A | LEU486 |
| A | CYS489 |
| A | HIS490 |
| A | GLN509 |
| A | ARG510 |
| A | SER511 |
| A | ASP513 |
| A | ASN521 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | binding site for residue NDP A 702 |
| Chain | Residue |
| A | VAL9 |
| A | ALA10 |
| A | ILE17 |
| A | ASN21 |
| A | GLY22 |
| A | LEU23 |
| A | TRP25 |
| A | GLY80 |
| A | ARG81 |
| A | LYS82 |
| A | THR83 |
| A | VAL102 |
| A | SER103 |
| A | SER104 |
| A | SER105 |
| A | ALA128 |
| A | VAL151 |
| A | GLY153 |
| A | ALA154 |
| A | GLY155 |
| A | LEU156 |
| A | VAL182 |
| A | BOD704 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue CB3 A 703 |
| Chain | Residue |
| A | LYS371 |
| A | ARG372 |
| A | PHE374 |
| A | GLU381 |
| A | ILE402 |
| A | ASN406 |
| A | ASP513 |
| A | LEU516 |
| A | GLY517 |
| A | PHE520 |
| A | ASN521 |
| A | TYR553 |
| A | ARG603 |
| A | ALA609 |
| A | UMP701 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue BOD A 704 |
| Chain | Residue |
| A | VAL8 |
| A | VAL9 |
| A | ALA10 |
| A | LEU23 |
| A | ASP31 |
| A | PHE32 |
| A | MET87 |
| A | PRO88 |
| A | VAL151 |
| A | TYR157 |
| A | THR172 |
| A | NDP702 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue UMP B 701 |
| Chain | Residue |
| A | ARG469 |
| A | ARG470 |
| B | ARG344 |
| B | LEU486 |
| B | CYS489 |
| B | HIS490 |
| B | GLN509 |
| B | ARG510 |
| B | SER511 |
| B | CYS512 |
| B | ASP513 |
| B | ASN521 |
| B | HIS551 |
| B | TYR553 |
| B | CB3703 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | binding site for residue NDP B 702 |
| Chain | Residue |
| B | GLY155 |
| B | LEU156 |
| B | ALA159 |
| B | VAL182 |
| B | BOD704 |
| B | VAL9 |
| B | ALA10 |
| B | ILE17 |
| B | GLY18 |
| B | ILE19 |
| B | ASN21 |
| B | GLY22 |
| B | LEU23 |
| B | TRP25 |
| B | ARG81 |
| B | LYS82 |
| B | THR83 |
| B | VAL102 |
| B | SER104 |
| B | ALA128 |
| B | SER129 |
| B | VAL151 |
| B | GLY152 |
| B | GLY153 |
| B | ALA154 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | binding site for residue CB3 B 703 |
| Chain | Residue |
| B | ARG372 |
| B | VAL373 |
| B | PHE374 |
| B | GLU381 |
| B | ILE402 |
| B | ASN406 |
| B | ASP513 |
| B | LEU516 |
| B | GLY517 |
| B | PHE520 |
| B | ASN521 |
| B | TYR553 |
| B | MET608 |
| B | ALA609 |
| B | UMP701 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue BOD B 704 |
| Chain | Residue |
| B | VAL8 |
| B | VAL9 |
| B | ALA10 |
| B | LEU23 |
| B | HIS27 |
| B | ASP31 |
| B | PHE32 |
| B | PHE35 |
| B | MET87 |
| B | PRO88 |
| B | VAL151 |
| B | THR172 |
| B | NDP702 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 24 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGinngLPWphlttDfkhFsrvT |
| Chain | Residue | Details |
| A | GLY16-THR39 |
| site_id | PS00091 |
| Number of Residues | 29 |
| Details | THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RrmLmtaWNpaaldema.....LpPCHllcQFyV |
| Chain | Residue | Details |
| A | ARG469-VAL497 |
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 | CYS489 | |
| B | CYS489 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | VAL8 | |
| A | ARG344 | |
| A | HIS490 | |
| A | GLN509 | |
| A | ASN521 | |
| A | HIS551 | |
| B | VAL8 | |
| B | ALA10 | |
| B | GLY16 | |
| B | ASP31 | |
| B | ARG81 | |
| A | ALA10 | |
| B | VAL102 | |
| B | GLY152 | |
| B | TYR157 | |
| B | THR172 | |
| B | ARG344 | |
| B | HIS490 | |
| B | GLN509 | |
| B | ASN521 | |
| B | HIS551 | |
| A | GLY16 | |
| A | ASP31 | |
| A | ARG81 | |
| A | VAL102 | |
| A | GLY152 | |
| A | TYR157 | |
| A | THR172 |
