Research workbench
Crystal structure of the delta-class glutathione transferase from musca domestica
Analyse Crystal structure of the delta-class glutathione transferase from musca… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZWP
- Type
- protein
- Length
- 414 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase 1
- EC
- 2.5.1.18
- UniProt
- P28338
- Ligands
- GSH
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 61% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase 1 (EC 2.5.1.18) | protein | 207 | 61% helix, 9% strand | P28338 |
Ligands and binding sites
- GSH · Glutathione · ligand · 2 copies · chains A, B
- FMT · Formic acid · additive · 11 copies · chains A, B
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 | 1084 | 0.77 | 0.79 | 76 | GSH, FMT |
| 2 | 138 | 0.41 | 0.74 | 27 | FMT |
| 3 | 91 | 0.36 | 0.75 | 19 | FMT |
Interfaces
1 interface between chains.
- A–B · 1501 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 5ZWP · Crystal structure of the delta-class glutathione transferase from Musca domestica · the same entry in another collection · chain A against A, TM-score 1.00
- P28338 · AlphaFold monomer V2.0 prediction for glutathione S-transferase 1 (P28338) · 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 P28338
- Elsewhere: RCSB PDB 5ZWP · PDBe 5ZWP · UniProt P28338
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.