Research workbench
Staphylococcus aureus dihydrofolate reductase complexed with NADPH and 2,4-diamino-5-[3-(3,4,5-TRIMETHOXYPHENYL)PENT-1-ynyl]-6- methylpyrimidine (UCP115A)
Analyse Staphylococcus aureus dihydrofolate reductase complexed with NADPH and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FQC
- Type
- protein
- Length
- 314 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trimethoprim-sensitive dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- Q2YY41
- Ligands
- NDP, 55V
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Trimethoprim-sensitive dihydrofolate reductase (EC 1.5.1.3) | protein | 157 | 20% helix, 36% strand | Q2YY41 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- 55V · 6-methyl-5-[3-methyl-3-(3,4,5-trimethoxyphenyl)but-1-yn-1-yl]pyrimidine-2,4-diamine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 376 | 0.68 | 0.81 | 37 | NDP, 55V |
| 2 | 404 | 0.68 | 0.80 | 38 | NDP, 55V |
| 3 | 220 | 0.50 | 0.76 | 36 | empty |
| 4 | 95 | 0.38 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 462 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3FQC · Staphylococcus aureus dihydrofolate reductase complexed with NADPH and… · 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 Q2YY41
- Elsewhere: RCSB PDB 3FQC · PDBe 3FQC · UniProt Q2YY41
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