Research workbench
Crystal structure of the wild type thioredoxin glutatione reductase from schistosoma mansoni in complex with auranofin
Analyse Crystal structure of the wild type thioredoxin glutatione reductase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H4K
- Type
- protein
- Length
- 588 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin glutathione reductase
- EC
- 1.6.4.5
- UniProt
- Q962Y6
- Ligands
- FAD, GSH, AU, K
- Pockets
- 6 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin glutathione reductase (EC 1.6.4.5) | protein | 588 | 37% helix, 24% strand | Q962Y6 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- GSH · Glutathione · ligand · chains A
- AU · Gold ion · metal · 3 copies · chains A
- K · Potassium ion · metal · chains A
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1159 | 0.80 | 0.81 | 120 | FAD, AU, K |
| 2 | 169 | 0.50 | 0.78 | 30 | empty |
| 3 | 109 | 0.44 | 0.78 | 17 | PG4 |
| 4 | 93 | 0.40 | 0.77 | 25 | empty |
| 5 | 79 | 0.38 | 0.77 | 17 | empty |
Compared structures
- 3H4K · Crystal structure of the wild type Thioredoxin glutatione reductase from Schistosoma… · the same entry in another collection · 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 Q962Y6
- Elsewhere: RCSB PDB 3H4K · PDBe 3H4K · UniProt Q962Y6
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