MolNFT v1 · #20383 · protein
Dihydrofolate reductase complexed with folate
1RD7: “Dihydrofolate reductase complexed with folate”. X-ray diffraction, 1 ligand (FOL), 2 pockets (best druggability 0.67). MolNFT v1 #20383 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1RD7
- Type
- protein
- Length
- 318 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- P0ABQ4
- Ligands
- FOL
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dihydrofolate reductase (EC 1.5.1.3) | protein | 159 | 25% helix, 35% strand | P0ABQ4 |
Ligands and binding sites
- FOL · Folic acid · ligand · 2 copies · chains A, B
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 570 | 0.67 | 0.77 | 44 | FOL |
| 2 | 506 | 0.66 | 0.77 | 36 | FOL |
Interfaces
1 interface between chains.
- A–B · 426 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct).
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 P0ABQ4
- Elsewhere: RCSB PDB 1RD7 · PDBe 1RD7 · UniProt P0ABQ4
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