Research workbench
Structure of onchocerca volvulus pi-class glutathione S-transferase
Analyse Structure of onchocerca volvulus pi-class glutathione S-transferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TU7
- Type
- protein
- Length
- 416 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase 2
- EC
- 2.5.1.18
- UniProt
- P46427
- Ligands
- GSH
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase 2 (EC 2.5.1.18) | protein | 208 | 59% helix, 10% strand | P46427 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 906 | 0.77 | 0.80 | 74 | GSH |
| 2 | 69 | 0.33 | 0.75 | 13 | GOL |
| 3 | 60 | 0.28 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1343 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 1TU7 · Structure of Onchocerca Volvulus Pi-class Glutathione S-transferase · the same entry in another collection · chain A against A, TM-score 1.00
- P46427 · AlphaFold monomer V2.0 prediction for glutathione S-transferase 2 (P46427) · 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 P46427
- Elsewhere: RCSB PDB 1TU7 · PDBe 1TU7 · UniProt P46427
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