MolNFT v1 · #89050 · protein
Human dihydrofolate reductase complexed with NADPH and P218
4DDR: “Human dihydrofolate reductase complexed with NADPH and P218”. X-ray diffraction, 2 ligands (NDP, MMV), 2 pockets (best druggability 0.75). MolNFT v1 #89050 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4DDR
- Type
- protein
- Length
- 186 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- P00374
- Ligands
- NDP, MMV
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase (EC 1.5.1.3) | protein | 186 | 22% helix, 32% strand | P00374 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- MMV · 3-(2-{3-[(2,4-diamino-6-ethylpyrimidin-5-yl) oxy]propoxy}phenyl)propanoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 387 | 0.75 | 0.85 | 47 | NDP, MMV |
| 2 | 50 | 0.32 | 0.77 | 19 | empty |
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 P00374
- Elsewhere: RCSB PDB 4DDR · PDBe 4DDR · UniProt P00374
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