Research workbench
Tetra-(5-fluorotryptophanyl)-glutathione transferase
Analyse Tetra-(5-fluorotryptophanyl)-glutathione transferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FWG
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetra-(5-fluorotryptophanyl)-glutathione transferase mu class
- EC
- 2.5.1.18
- UniProt
- P04905
- Ligands
- GPR
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tetra-(5-fluorotryptophanyl)-glutathione transferase mu class (EC 2.5.1.18) | protein | 217 | 51% helix, 9% strand | P04905 |
Ligands and binding sites
- GPR · (9R,10R)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1176 | 0.74 | 0.77 | 84 | GPR |
| 2 | 170 | 0.59 | 0.83 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1450 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (nonstandard).
Compared structures
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 P04905
- Elsewhere: RCSB PDB 5FWG · PDBe 5FWG · UniProt P04905
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