Research workbench
Arabidopsis thaliana GSTU23, gsh bound
Analyse Arabidopsis thaliana GSTU23, gsh bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EP7
- Type
- protein
- Length
- 424 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase U23
- EC
- 2.5.1.18
- UniProt
- Q9M9F1
- Ligands
- GSH, MG
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase U23 (EC 2.5.1.18) | protein | 210 | 59% helix, 9% strand | Q9M9F1 |
| B | Glutathione S-transferase U23 (EC 2.5.1.18) | protein | 214 | 60% helix, 9% strand | Q9M9F1 |
Ligands and binding sites
- GSH · Glutathione · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 917 | 0.81 | 0.83 | 77 | GSH, GOL |
| 2 | 135 | 0.45 | 0.77 | 27 | MG, GOL |
| 3 | 98 | 0.40 | 0.77 | 22 | empty |
| 4 | 120 | 0.38 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1184 Ų buried · 17 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 Q9M9F1
- Elsewhere: RCSB PDB 6EP7 · PDBe 6EP7 · UniProt Q9M9F1
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