Research workbench
Crystal Structure Of glutathione transferase YghU from Streptococcus pneumoniae ATCC 700669, complexed with glutathione, Target EFI-507284
Analyse Crystal Structure Of glutathione transferase YghU from Streptococcus pneumoniae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PUA
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.708
- Source
- Streptococcus pneumoniae
- Molecule
- glutathione S-transferase
- EC
- 2.5.1.18
- UniProt
- B8ZLL4
- Ligands
- GSH
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · resolution 1.708 · 1 distinct chain · 51% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | glutathione S-transferase (EC 2.5.1.18) | protein | 261 | 51% helix, 10% strand | B8ZLL4 |
Ligands and binding sites
- GSH · Glutathione · ligand · 2 copies · 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 | 508 | 0.64 | 0.77 | 48 | GSH |
Compared structures
- 4PUA · Crystal structure of glutathione transferase yghu from streptococcus pneumoniae atcc… · 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 B8ZLL4
- Elsewhere: RCSB PDB 4PUA · PDBe 4PUA · UniProt B8ZLL4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.