Research workbench
Glutathionyl-hydroquinone reductase, yqjg, of E.COLI complexed with gsh
Analyse Glutathionyl-hydroquinone reductase, yqjg, of E.COLI complexed with gsh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G0L
- Type
- protein
- Length
- 653 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P42620
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 327 | — | P42620 |
| B | — | protein | 326 | — | P42620 |
Compared structures
- 4G0L · Glutathionyl-hydroqui Reductase, YqjG, of E.coli complexed with GSH · 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 0.95
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 4G0L · PDBe 4G0L · UniProt P42620
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