MolNFT v1 · #153558 · protein
Crystal structure of glutathione S-transferase complexed and modified with glutathione
6JI6 · Glutathione S-transferase class-mu 26 kda isozyme: “Crystal structure of glutathione S-transferase complexed and modified with glutathione”. X-ray diffraction, 1 ligand (GSH), 1 pocket (best druggability 0.52). MolNFT v1 #153558 on…
- PDB
- 6JI6
- Type
- protein
- Length
- 215 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase class-mu 26 kda isozyme
- EC
- 2.5.1.18
- UniProt
- P08515
- Ligands
- GSH
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase class-mu 26 kda isozyme (EC 2.5.1.18) | protein | 215 | 53% helix, 9% strand | P08515 |
Ligands and binding sites
- GSH · Glutathione · ligand · 4 copies · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.52 | 0.83 | 24 | ACT, TRS |
Modifications
Observed in the structure: 3 covalent (covalent ligand).
Compared structures
- 6JI6 · Crystal structure of glutathione S-transferase complexed and modified with glutathione · the same entry in another collection · chain A against A, TM-score 1.00
- P08515 · AlphaFold monomer V2.0 prediction for glutathione S-transferase class-mu 26 kda isozyme… · 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 P08515
- Elsewhere: RCSB PDB 6JI6 · PDBe 6JI6 · UniProt P08515
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