Research workbench
Crystal structure of glutathione S-transferase Tau7 from Salix lindleyana in complex with GSH
Analyse Crystal structure of glutathione S-transferase Tau7 from Salix lindleyana in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8JZK
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.55004
- Source
- Salix lindleyana
- Molecule
- glutathione transferase
- UniProt
- A0A5N5L538
- Ligands
- GSH
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · resolution 2.55004 · 1 distinct chain · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | glutathione transferase | protein | 214 | 59% helix, 8% strand | A0A5N5L538 |
Ligands and binding sites
- GSH · Glutathione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 160 | 0.43 | 0.74 | 18 | empty |
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 A0A5N5L538
- Elsewhere: RCSB PDB 8JZK · PDBe 8JZK · UniProt A0A5N5L538
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