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Crystal structure of glutahtione s-transferase homolog from yersinia pestis, target EFI-501894, with bound glutathione
Analyse Crystal structure of glutahtione s-transferase homolog from yersinia pestis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G9H
- Type
- protein
- Length
- 404 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Yersinia pestis
- Molecule
- Glutathione S-transferase
- UniProt
- Q8D0L3
- Ligands
- GSH
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 54% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase | protein | 202 | 54% helix, 10% strand | Q8D0L3 |
Ligands and binding sites
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 | 982 | 0.78 | 0.80 | 94 | GSH |
| 2 | 143 | 0.41 | 0.74 | 28 | empty |
| 3 | 124 | 0.41 | 0.75 | 29 | GOL |
Interfaces
1 interface between chains.
- A–B · 1634 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 4G9H · Crystal structure of glutahtione S-transferase homolog from yersinia pestis, target… · 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 Q8D0L3
- Elsewhere: RCSB PDB 4G9H · PDBe 4G9H · UniProt Q8D0L3
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