Research workbench
Crystal structure of GTT2 from saccharomyces cerevisiae in complex with glutathione sulfnate
Analyse Crystal structure of GTT2 from saccharomyces cerevisiae in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ERG
- 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
- Q12390
- Ligands
- GTS
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase 2 (EC 2.5.1.18) | protein | 208 | 57% helix, 8% strand | Q12390 |
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
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 | 1072 | 0.84 | 0.85 | 88 | GTS |
| 2 | 199 | 0.46 | 0.74 | 32 | empty |
| 3 | 128 | 0.41 | 0.75 | 31 | empty |
| 4 | 55 | 0.29 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1756 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3ERG · Crystal structure of Gtt2 from Saccharomyces cerevisiae in complex with glutathione… · the same entry in another collection · chain A against A, TM-score 1.00
- Q12390 · AlphaFold monomer V2.0 prediction for glutathione S-transferase 2 (Q12390) · 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 Q12390
- Elsewhere: RCSB PDB 3ERG · PDBe 3ERG · UniProt Q12390
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