Research workbench
ARABIDOPSIS THALIANA GSTU23, reduced
Analyse ARABIDOPSIS THALIANA GSTU23, reduced in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EP6
- Type
- protein
- Length
- 428 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.592
- Source
- Arabidopsis thaliana
- Molecule
- Glutathione S-transferase U23
- EC
- 2.5.1.18
- UniProt
- Q9M9F1
- Ligands
- MG
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · resolution 1.592 · 2 distinct chains · 58% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase U23 (EC 2.5.1.18) | protein | 212 | 58% helix, 9% strand | Q9M9F1 |
| B | Glutathione S-transferase U23 (EC 2.5.1.18) | protein | 216 | 58% helix, 9% strand | Q9M9F1 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- GOL · Glycerol · additive · 3 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 | 87 | empty |
| 2 | 134 | 0.47 | 0.77 | 28 | GOL, MG |
| 3 | 118 | 0.44 | 0.77 | 31 | MG, GOL |
| 4 | 103 | 0.37 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1190 Ų buried · 16 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 6EP6 · PDBe 6EP6 · UniProt Q9M9F1
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