Research workbench
Glutathionyl-hydroquinone reductase, yqjg of escherichia COLI
Analyse Glutathionyl-hydroquinone reductase, yqjg of escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G0I
- Type
- protein
- Length
- 654 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein yqjg
- UniProt
- P42620
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein yqjg | protein | 327 | 40% helix, 9% strand | P42620 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 12 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.68 | 0.91 | 32 | empty |
| 2 | 509 | 0.67 | 0.78 | 51 | SO4 |
| 3 | 516 | 0.67 | 0.78 | 51 | SO4 |
| 4 | 57 | 0.27 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1200 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 4G0I · Glutathionyl-Hydroqui Reductase, YqjG of Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P42620 · AlphaFold monomer V2.0 prediction for glutathionyl-hydroquinone reductase yqjg (P42620) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P42620
- Elsewhere: RCSB PDB 4G0I · PDBe 4G0I · UniProt P42620
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