MolNFT v1 · #25036 · protein
Dihydrofolate reductase
1VDR: “Dihydrofolate reductase”. X-ray diffraction, 1 ligand (PO4), 2 pockets (best druggability 0.79). MolNFT v1 #25036 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1VDR
- Type
- protein
- Length
- 311 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- P15093
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase (EC 1.5.1.3) | protein | 157 | 23% helix, 36% strand | P15093 |
| B | Dihydrofolate reductase (EC 1.5.1.3) | protein | 154 | 23% helix, 34% strand | P15093 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 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 | 832 | 0.79 | 0.82 | 80 | PO4 |
| 2 | 268 | 0.64 | 0.81 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 697 Ų buried · 12 hydrogen bonds · protein-protein
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 P15093
- Elsewhere: RCSB PDB 1VDR · PDBe 1VDR · UniProt P15093
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