MolNFT v1 · #175543 · protein
Wild type plasmodium falciparum dihydrofolate reductase-thymidylate synthase (pfdhfr-ts), fragment 263, NADP+, dump
7CTY · Bifunctional dihydrofolate reductase-thymidylate synthase: “Wild type plasmodium falciparum dihydrofolate reductase-thymidylate synthase (pfdhfr-ts), fragment 263…”. X-ray diffraction, 3 ligands (GF3, NDP, PO4), 17 pockets (best…
- PDB
- 7CTY
- Type
- protein
- Length
- 1,041 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional dihydrofolate reductase-thymidylate synthase
- UniProt
- A7UD81
- Ligands
- GF3, NDP, PO4
- Pockets
- 17 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional dihydrofolate reductase-thymidylate synthase | protein | 529 | 31% helix, 25% strand | A7UD81 |
| B | Bifunctional dihydrofolate reductase-thymidylate synthase | protein | 512 | 29% helix, 24% strand | A7UD81 |
Ligands and binding sites
- GF3 · spiro[1H-2-benzofuran-3,4'-piperidine] · ligand · 2 copies · chains A, B
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 419 | 0.74 | 0.84 | 40 | GF3 |
| 2 | 485 | 0.72 | 0.82 | 49 | NDP, GF3 |
| 3 | 736 | 0.72 | 0.78 | 66 | PO4 |
| 4 | 675 | 0.72 | 0.78 | 64 | PO4 |
| 5 | 122 | 0.52 | 0.81 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 4207 Ų buried · 47 hydrogen bonds · protein-protein
Compared structures
- 7CTY · Wild type plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS)… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A7UD81
- Elsewhere: RCSB PDB 7CTY · PDBe 7CTY · UniProt A7UD81
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