3DG8
Quadruple mutant (N51I+C59R+S108N+I164L) Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) complexed with RJF670, NADPH, and dUMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0050661 | molecular_function | NADP binding |
| B | 0004146 | molecular_function | dihydrofolate reductase activity |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0050661 | molecular_function | NADP binding |
| C | 0004799 | molecular_function | thymidylate synthase activity |
| C | 0006231 | biological_process | dTMP biosynthetic process |
| C | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
| D | 0004799 | molecular_function | thymidylate synthase activity |
| D | 0006231 | biological_process | dTMP biosynthetic process |
| D | 0016741 | molecular_function | transferase activity, transferring one-carbon groups |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE RJ6 A 609 |
| Chain | Residue |
| A | ILE14 |
| A | TYR170 |
| A | NDP610 |
| A | CYS15 |
| A | LEU46 |
| A | ASP54 |
| A | PHE58 |
| A | ASN108 |
| A | ILE112 |
| A | LEU119 |
| A | LEU164 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NDP A 610 |
| Chain | Residue |
| A | CYS15 |
| A | ALA16 |
| A | LEU40 |
| A | GLY44 |
| A | VAL45 |
| A | GLY105 |
| A | ARG106 |
| A | THR107 |
| A | ASN108 |
| A | LEU127 |
| A | SER128 |
| A | ARG129 |
| A | THR130 |
| A | ASN144 |
| A | VAL146 |
| A | LEU164 |
| A | GLY165 |
| A | GLY166 |
| A | SER167 |
| A | VAL168 |
| A | VAL169 |
| A | TYR170 |
| A | GLU172 |
| A | VAL195 |
| A | RJ6609 |
| A | HOH1073 |
| A | HOH1151 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE UMP C 611 |
| Chain | Residue |
| C | ARG345 |
| C | CYS490 |
| C | HIS491 |
| C | GLN509 |
| C | ARG510 |
| C | SER511 |
| C | ASP513 |
| C | GLY517 |
| C | ASN521 |
| C | HIS551 |
| C | TYR553 |
| C | HOH1048 |
| D | ARG470 |
| D | ARG471 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE RJ6 B 609 |
| Chain | Residue |
| B | ILE14 |
| B | LEU46 |
| B | ASP54 |
| B | PHE58 |
| B | ASN108 |
| B | ILE112 |
| B | LEU119 |
| B | LEU164 |
| B | TYR170 |
| B | NDP610 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NDP B 610 |
| Chain | Residue |
| B | CYS15 |
| B | ALA16 |
| B | LEU40 |
| B | GLY44 |
| B | GLY105 |
| B | ARG106 |
| B | THR107 |
| B | ASN108 |
| B | LEU127 |
| B | SER128 |
| B | ARG129 |
| B | THR130 |
| B | ASN144 |
| B | LYS145 |
| B | LEU164 |
| B | GLY165 |
| B | GLY166 |
| B | SER167 |
| B | VAL168 |
| B | VAL169 |
| B | TYR170 |
| B | GLU172 |
| B | RJ6609 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE UMP D 611 |
| Chain | Residue |
| C | ARG470 |
| C | ARG471 |
| D | CYS490 |
| D | HIS491 |
| D | GLN509 |
| D | ARG510 |
| D | SER511 |
| D | ASP513 |
| D | GLY517 |
| D | ASN521 |
| D | HIS551 |
| D | TYR553 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 24 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GLGnkgvLPWkcislDmkyFravT |
| Chain | Residue | Details |
| A | GLY39-THR62 |
| site_id | PS00091 |
| Number of Residues | 29 |
| Details | THYMIDYLATE_SYNTHASE Thymidylate synthase active site. RriLlcaWNvkdldqma.....LpPCHilcQFyV |
| Chain | Residue | Details |
| C | ARG470-VAL498 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| C | CYS490 | |
| A | GLY165 | |
| A | TYR170 | |
| B | ILE14 | |
| B | ALA16 | |
| B | GLY39 | |
| B | ASP54 | |
| B | ARG106 | |
| B | ASN108 | |
| B | SER128 | |
| B | ASN144 | |
| D | CYS490 | |
| B | LEU164 | |
| B | GLY165 | |
| B | TYR170 | |
| A | GLY39 | |
| A | ASP54 | |
| A | ARG106 | |
| A | ASN108 | |
| A | SER128 | |
| A | ASN144 | |
| A | LEU164 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| C | ARG345 | |
| D | HIS551 | |
| C | HIS491 | |
| C | GLN509 | |
| C | ASN521 | |
| C | HIS551 | |
| D | ARG345 | |
| D | HIS491 | |
| D | GLN509 | |
| D | ASN521 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| C | ASN521 | |
| C | CYS490 | |
| C | SER524 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| D | ASN521 | |
| D | CYS490 | |
| D | SER524 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| A | ASP54 | |
| A | LEU46 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b02 |
| Chain | Residue | Details |
| B | ASP54 | |
| B | LEU46 |
