Research workbench
Structure of porcine class pi glutathione S-transferase
Analyse Structure of porcine class pi 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
- 2GSR
- Type
- protein
- Length
- 414 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Class pi GST glutathione S-transferase
- EC
- 2.5.1.18
- UniProt
- P80031
- Ligands
- GTS
- Pockets
- 5 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Class pi GST glutathione S-transferase (EC 2.5.1.18) | protein | 207 | 60% helix, 8% strand | P80031 |
Ligands and binding sites
- GTS · Glutathione sulfonic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 808 | 0.76 | 0.80 | 90 | GTS |
| 2 | 67 | 0.44 | 0.82 | 15 | empty |
| 3 | 107 | 0.38 | 0.74 | 16 | empty |
| 4 | 95 | 0.36 | 0.74 | 14 | empty |
| 5 | 50 | 0.25 | 0.73 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1405 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 P80031
- Elsewhere: RCSB PDB 2GSR · PDBe 2GSR · UniProt P80031
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