Research workbench
Crystal structure of human kappa class glutathione transferase
Analyse Crystal structure of human kappa class glutathione transferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YZX
- Type
- protein
- Length
- 436 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase kappa 1
- EC
- 2.5.1.18
- UniProt
- Q9Y2Q3
- Ligands
- GSF
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase kappa 1 (EC 2.5.1.18) | protein | 218 | 56% helix, 12% strand | Q9Y2Q3 |
Ligands and binding sites
- GSF · L-gamma-glutamyl-3-sulfino-L-alanylglycine · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 801 | 0.86 | 0.88 | 68 | GSF |
| 2 | 169 | 0.81 | 0.96 | 26 | empty |
| 3 | 52 | 0.35 | 0.78 | 15 | empty |
| 4 | 62 | 0.33 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1425 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 1YZX · Crystal structure of human kappa class glutathione transferase · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y2Q3 · AlphaFold monomer V2.0 prediction for glutathione S-transferase kappa 1 (Q9Y2Q3) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9Y2Q3
- Elsewhere: RCSB PDB 1YZX · PDBe 1YZX · UniProt Q9Y2Q3
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