Research workbench
Quadruple MUTANT(N51I+C59R+S108N+I164L) plasmodium falciparum dihydrofolate reductase-thymidylate SYNTHASE(PFDHFR-ts) complexed with QN254, NADPH, and dump
Analyse Quadruple MUTANT(N51I+C59R+S108N+I164L) plasmodium falciparum dihydrofolate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JSU
- Type
- protein
- Length
- 1,087 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase-thymidylate synthase
- EC
- 1.5.1.3, 2.1.1.45
- UniProt
- A7UD79
- Ligands
- KA5, NDP, UMP
- Pockets
- 18 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase-thymidylate synthase (EC 1.5.1.3, 2.1.1.45) | protein | 545 | 31% helix, 25% strand | A7UD79 |
| B | Dihydrofolate reductase-thymidylate synthase (EC 1.5.1.3, 2.1.1.45) | protein | 542 | 31% helix, 25% strand | A7UD79 |
Ligands and binding sites
- KA5 · 5-chloro-N~6~-(2,5-dimethoxybenzyl)quinazoline-2,4,6-triamine · ligand · 2 copies · chains A, B
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- UMP · 2'-deoxyuridine 5'-monophosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.73 | 0.82 | 45 | KA5, NDP |
| 2 | 475 | 0.72 | 0.81 | 46 | KA5, NDP |
| 3 | 658 | 0.70 | 0.78 | 66 | UMP |
| 4 | 603 | 0.70 | 0.78 | 55 | UMP |
| 5 | 277 | 0.53 | 0.75 | 36 | empty |
Interfaces
1 interface between chains.
- A–B · 4159 Ų buried · 50 hydrogen bonds · protein-protein
Compared structures
- 3JSU · Quadruple mutant(N51I+C59R+S108N+I164L) plasmodium falciparum dihydrofolate… · 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 A7UD79
- Elsewhere: RCSB PDB 3JSU · PDBe 3JSU · UniProt A7UD79
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