Research workbench
Human glutathione transferase O2 with glutathione -new crystal form
Analyse Human glutathione transferase O2 with glutathione -new crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QAG
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase omega-2
- EC
- 2.5.1.18
- UniProt
- Q9H4Y5
- Ligands
- GSH
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase omega-2 (EC 2.5.1.18) | protein | 238 | 53% helix, 8% strand | Q9H4Y5 |
Ligands and binding sites
- GSH · Glutathione · ligand · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
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 | 251 | 0.61 | 0.80 | 31 | GSH, EDO |
| 2 | 54 | 0.35 | 0.78 | 14 | empty |
| 3 | 53 | 0.34 | 0.78 | 13 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 3QAG · Human Glutathione Transferase O2 with glutathione -new crystal form · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H4Y5 · AlphaFold monomer V2.0 prediction for glutathione S-transferase omega-2 (Q9H4Y5) · 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 Q9H4Y5
- Elsewhere: RCSB PDB 3QAG · PDBe 3QAG · UniProt Q9H4Y5
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