Research workbench
Human glutathione reductase A34E, R37W mutant, mixed disulfide between trypanothione and the enzyme
Analyse Human glutathione reductase A34E, R37W mutant, mixed disulfide between… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GRT
- 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, GCG
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione reductase (EC 1.6.4.2) | protein | 461 | 32% helix, 25% strand | P00390 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- GCG · Bis(gamma-glutamyl-cysteinyl-glycinyl)spermidine · 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 | 1094 | 0.77 | 0.79 | 109 | FAD |
| 2 | 132 | 0.58 | 0.84 | 27 | empty |
| 3 | 70 | 0.36 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 4GRT · Human glutathione reductase A34E, R37W mutant, mixed disulfide between trypanothione and… · 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 4GRT · PDBe 4GRT · UniProt P00390
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