Research workbench
Glutathione S-transferase in complex with glutathione
Analyse Glutathione S-transferase in complex with glutathione in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AQW
- Type
- protein
- Length
- 836 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase
- EC
- 2.5.1.18
- UniProt
- P09211
- Ligands
- GSH
- Pockets
- 10 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Glutathione S-transferase (EC 2.5.1.18) | protein | 209 | 62% helix, 9% strand | P09211 |
Ligands and binding sites
- GSH · Glutathione · ligand · 4 copies · chains A, B, C, D
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 638 | 0.72 | 0.79 | 81 | GSH |
| 2 | 585 | 0.71 | 0.79 | 71 | GSH |
| 3 | 198 | 0.50 | 0.76 | 31 | empty |
| 4 | 102 | 0.40 | 0.76 | 17 | empty |
| 5 | 89 | 0.36 | 0.75 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1295 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1264 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 269 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1AQW · Glutathione S-transferase in complex with glutathione · 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 P09211
- Elsewhere: RCSB PDB 1AQW · PDBe 1AQW · UniProt P09211
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