Research workbench
Crystal structure of a glutathione S-transferase from pichia kudriavzevii (issatchenkia orientalis), target efi-501747
Analyse Crystal structure of a glutathione S-transferase from pichia kudriavzevii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O92
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase
- UniProt
- Q9Y727
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase | protein | 196 | 57% helix, 9% strand | Q9Y727 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.50 | 0.86 | 15 | empty |
| 2 | 94 | 0.38 | 0.76 | 14 | empty |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 4O92 · Crystal structure of a Glutathione S-transferase from Pichia kudriavzevii (Issatchenkia… · the same entry in another collection · 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 Q9Y727
- Elsewhere: RCSB PDB 4O92 · PDBe 4O92 · UniProt Q9Y727
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.