Research workbench
Crystal structure of a glutathione S-transferase SBGSTU7 from salix babylonica in complex with glutathione
Analyse Crystal structure of a glutathione S-transferase SBGSTU7 from salix babylonica… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DWE
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase
- UniProt
- A0A4Y5R087
- Ligands
- GSH
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase | protein | 212 | 59% helix, 9% strand | A0A4Y5R087 |
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
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.61 | 0.79 | 36 | GSH |
| 2 | 75 | 0.33 | 0.75 | 20 | empty |
| 3 | 54 | 0.29 | 0.75 | 17 | empty |
Compared structures
- 7DWE · Crystal structure of a glutathione S-transferase SbGSTU7 from Salix babylonica 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 A0A4Y5R087
- Elsewhere: RCSB PDB 7DWE · PDBe 7DWE · UniProt A0A4Y5R087
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