Research workbench
Human glutathione reductase modified by diglutathione-dinitroso-iron
Analyse Human glutathione reductase modified by diglutathione-dinitroso-iron in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DNC
- Type
- protein
- Length
- 461 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione reductase
- EC
- 1.6.4.2
- UniProt
- P00390
- Ligands
- FAD, GSH, PO4
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione reductase (EC 1.6.4.2) | protein | 461 | 34% helix, 25% strand | P00390 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- GSH · Glutathione · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 794 | 0.77 | 0.81 | 99 | FAD |
| 2 | 123 | 0.56 | 0.83 | 29 | empty |
| 3 | 80 | 0.39 | 0.78 | 17 | PO4 |
| 4 | 51 | 0.33 | 0.77 | 14 | GSH |
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, oxidation).
Compared structures
- 1DNC · Human glutathione reductase modified by diglutathione-dinitroso-iron · the same entry in another collection · chain A against A, TM-score 1.00
- P00390 · AlphaFold monomer V2.0 prediction for glutathione reductase, mitochondrial (P00390) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P00390
- Elsewhere: RCSB PDB 1DNC · PDBe 1DNC · UniProt P00390
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