MolNFT v1 · #164230 · protein
Crystal structure of glutathione transferase omega 2C from trametes versicolor in complex with oxyresveratrol
6SR9 · Uncharacterized protein: “Crystal structure of glutathione transferase omega 2C from trametes versicolor in complex with oxyresveratrol”. X-ray diffraction, 2 ligands (GSH, EZE), 2 pockets (best druggability 0.67). MolNFT v1 #164230…
- PDB
- 6SR9
- Type
- protein
- Length
- 468 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- R7S7J5
- Ligands
- GSH, EZE
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 235 | 56% helix, 8% strand | R7S7J5 |
| B | Uncharacterized protein | protein | 233 | 53% helix, 9% strand | R7S7J5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 611 | 0.67 | 0.77 | 58 | GSH |
| 2 | 239 | 0.54 | 0.77 | 29 | EZE |
Interfaces
1 interface between chains.
- A–B · 283 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 6SR9 · Crystal structure of glutathione transferase Omega 2C from Trametes versicolor in complex… · 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 R7S7J5
- Elsewhere: RCSB PDB 6SR9 · PDBe 6SR9 · UniProt R7S7J5
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