MolNFT v1 · #17251 · protein
Crystal structure of plasmodium falciparum glutathione reductase
1ONF: “Crystal structure of plasmodium falciparum glutathione reductase”. X-ray diffraction, 1 ligand (FAD), 3 pockets (best druggability 0.77). MolNFT v1 #17251 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1ONF
- Type
- protein
- Length
- 439 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione reductase
- EC
- 1.8.1.7
- UniProt
- Q94655
- Ligands
- FAD
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione reductase (EC 1.8.1.7) | protein | 439 | 34% helix, 23% strand | Q94655 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1129 | 0.77 | 0.79 | 122 | FAD |
| 2 | 236 | 0.60 | 0.80 | 30 | empty |
| 3 | 83 | 0.34 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q94655
- Elsewhere: RCSB PDB 1ONF · PDBe 1ONF · UniProt Q94655
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