MolNFT v1 · #38069 · protein
Molecular structure at 1.8 ångströms of mouse liver class pi glutathione S-transferase complexed with S-(P-NITROBENZYL)GLUTATHIONE and other inhibitors
2GLR · Glutathione S-transferase yfyf: “Molecular structure at 1.8 ångströms of mouse liver class pi glutathione S-transferase complexed with…”. X-ray diffraction, 1 ligand (GTX), 5 pockets (best druggability 0.73). MolNFT v1 #38069 on…
- PDB
- 2GLR
- Type
- protein
- Length
- 418 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase yfyf
- EC
- 2.5.1.18
- UniProt
- P19157
- Ligands
- GTX
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase yfyf (EC 2.5.1.18) | protein | 209 | 61% helix, 8% strand | P19157 |
Ligands and binding sites
- GTX · S-hexylglutathione · 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 | 723 | 0.73 | 0.79 | 81 | GTX |
| 2 | 71 | 0.38 | 0.78 | 18 | empty |
| 3 | 88 | 0.36 | 0.76 | 21 | empty |
| 4 | 78 | 0.36 | 0.76 | 14 | empty |
| 5 | 59 | 0.28 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1356 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2GLR · Molecular structure at 1.8 ångströms of mouse liver class pi glutathione S-transferase… · the same entry in another collection · chain A against A, TM-score 1.00
- P19157 · AlphaFold monomer V2.0 prediction for glutathione S-transferase P 1 (P19157) · 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 P19157
- Elsewhere: RCSB PDB 2GLR · PDBe 2GLR · UniProt P19157
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.