Research workbench
Arabidopsis thaliana GSTF9, gsh and gsoh bound
Analyse Arabidopsis thaliana GSTF9, gsh and gsoh bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EZY
- Type
- protein
- Length
- 423 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase F9
- EC
- 2.5.1.18
- UniProt
- O80852
- Ligands
- GSH, GS8, BR
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 211 | 60% helix, 9% strand | O80852 |
| B | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 212 | 58% helix, 8% strand | O80852 |
Ligands and binding sites
- GSH · Glutathione · ligand · chains A, B
- GS8 · S-Hydroxy-Glutathione · ligand · chains B
- BR · Bromide ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 994 | 0.74 | 0.77 | 73 | GSH, GS8 |
| 2 | 56 | 0.26 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1374 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
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 O80852
- Elsewhere: RCSB PDB 6EZY · PDBe 6EZY · UniProt O80852
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