MolNFT v1 · #64029 · protein
S. aureus DHFR complexed with NADPH and iclaprim
3FRF · Dihydrofolate reductase: “S. aureus DHFR complexed with NADPH and iclaprim”. X-ray diffraction, 2 ligands (NDP, XCF), 1 pocket (best druggability 0.68). MolNFT v1 #64029 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3FRF
- Type
- protein
- Length
- 158 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- P0A017
- Ligands
- NDP, XCF
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Dihydrofolate reductase (EC 1.5.1.3) | protein | 158 | 18% helix, 37% strand | P0A017 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains X
- XCF · 5-[[(2R)-2-cyclopropyl-7,8-dimethoxy-2H-chromen-5-yl]methyl]pyrimidine-2,4-diamine · ligand · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.68 | 0.82 | 35 | NDP, XCF |
Compared structures
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 P0A017
- Elsewhere: RCSB PDB 3FRF · PDBe 3FRF · UniProt P0A017
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