Research workbench
Mouse C14A glutathione-S-transferase mutant in complex with S-hexyl glutathione
Analyse Mouse C14A glutathione-S-transferase mutant in complex with S-hexyl glutathione in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OA7
- Type
- protein
- Length
- 418 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase P 1
- EC
- 2.5.1.18
- UniProt
- P19157
- Ligands
- GTX
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase P 1 (EC 2.5.1.18) | protein | 209 | 59% helix, 9% strand | P19157 |
Ligands and binding sites
- GTX · S-hexylglutathione · ligand · 2 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 | 755 | 0.74 | 0.79 | 88 | GTX |
| 2 | 110 | 0.39 | 0.75 | 19 | empty |
| 3 | 101 | 0.37 | 0.74 | 23 | empty |
| 4 | 59 | 0.30 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1326 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2OA7 · Mouse C14A Glutathione-S-Transferase Mutant in Complex with S-hexyl glutathione · the same entry in another collection · chain A against A, TM-score 1.00
- P19157 · AlphaFold monomer V2.0 prediction for glutathione S-transferase P 1 (P19157) · a predicted model of the same protein · 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 P19157
- Elsewhere: RCSB PDB 2OA7 · PDBe 2OA7 · UniProt P19157
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