3JSU
Quadruple mutant(N51I+C59R+S108N+I164L) plasmodium falciparum dihydrofolate reductase-thymidylate synthase(PFDHFR-TS) complexed with QN254, NADPH, and dUMP
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | Dihydrofolate reductase-thymidylate synthase | polymer | 608 | 71908.1 | 2 | UniProt (A7UD79) Pfam (PF00186) Pfam (PF00303) UniProt (by SIFTS) (D9N170) | Plasmodium falciparum | Bifunctional dihydrofolate reductase-thymidylate synthase |
| 2 | C, F (A, B) | 5-chloro-N~6~-(2,5-dimethoxybenzyl)quinazoline-2,4,6-triamine | non-polymer | 359.8 | 2 | Chemie (KA5) | |||
| 3 | D, G (A, B) | NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE | non-polymer | 745.4 | 2 | Chemie (NDP) | |||
| 4 | E, H (A, B) | 2'-DEOXYURIDINE 5'-MONOPHOSPHATE | non-polymer | 308.2 | 2 | Chemie (UMP) | |||
| 5 | I, J (A, B) | water | water | 18.0 | 251 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 608 (UniProt: A7UD79)
| PDB | External Database | Details |
|---|---|---|
| Ile 51 | Asn 51 | engineered mutation |
| Arg 59 | Tyr 59 | engineered mutation |
| Asn 108 | Ser 108 | engineered mutation |
| Leu 164 | Ile 164 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 143816.3 | |
| Non-Polymers* | Number of molecules | 6 |
| Total formula weight | 2826.8 | |
| All* | Total formula weight | 146643.1 |
