Research workbench
Arabidopsis thaliana GSTF9, GSO3 bound
Analyse Arabidopsis thaliana GSTF9, GSO3 bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F05
- Type
- protein
- Length
- 2,012 residues
- Chains
- 10
- 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
- GTS, CL
- Pockets
- 12 · best druggability 0.72
Structure
x-ray diffraction · 10 distinct chains · 58% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 204 | 57% helix, 9% strand | O80852 |
| B | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 205 | 60% helix, 8% strand | O80852 |
| C | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 202 | 58% helix, 8% strand | O80852 |
| D | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 199 | 57% helix, 8% strand | O80852 |
| E | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 201 | 60% helix, 8% strand | O80852 |
| F | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 203 | 57% helix, 8% strand | O80852 |
| G | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 198 | 58% helix, 7% strand | O80852 |
| H | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 201 | 59% helix, 8% strand | O80852 |
| I | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 206 | 60% helix, 8% strand | O80852 |
| J | Glutathione S-transferase F9 (EC 2.5.1.18) | protein | 193 | 55% helix, 7% strand | O80852 |
Ligands and binding sites
- GTS · Glutathione sulfonic acid · ligand · 10 copies · chains A, B, C, D, E, F, J, G, H, I
- CL · Chloride ion · ion · 9 copies · chains A, B, C, D, E, F, G, H, I
- GOL · Glycerol · additive · 4 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 927 | 0.72 | 0.76 | 75 | GTS |
| 2 | 491 | 0.71 | 0.81 | 50 | GOL |
| 3 | 788 | 0.69 | 0.76 | 71 | GTS |
| 4 | 733 | 0.68 | 0.76 | 83 | GTS |
| 5 | 564 | 0.65 | 0.76 | 58 | GTS |
Interfaces
11 interfaces between chains.
- D–E · 1382 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 1364 Ų buried · 21 hydrogen bonds · protein-protein
- G–H · 1346 Ų buried · 19 hydrogen bonds · protein-protein
- F–J · 1342 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 460 Ų buried · 12 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 6F05 · PDBe 6F05 · UniProt O80852
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